BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30327

Title: NMR solution structure of Rtt103 (RTT) protein using two 4D-spectra   PubMed: 29374165

Deposition date: 2017-08-03 Original release date: 2018-01-29

Authors: Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.

Citation: Evangelidis, T.; Nerli, S.; Novacek, J.; Brereton, A.; Karplus, P.; Dotas, R.; Venditti, V.; Sgourakis, N.; Tripsianes, K.. "Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra"  Nat. Commun. 9, 384-384 (2018).

Assembly members:
Regulator of Ty1 transposition protein 103, polymer, 138 residues, 16132.574 Da.

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

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

Entity Sequences (FASTA):
Regulator of Ty1 transposition protein 103: SEQFTTKLNTLEDSQESISS ASKWLLLQYRDAPKVAEMWK EYMLRPSVNTRRKLLGLYLM NHVVQQAKGQKIIQFQDSFG KVAAEVLGRINQEFPRDLKK KLSRVVNILKERNIFSKQVV NDIERSLAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts459
15N chemical shifts144
1H chemical shifts978

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 138 residues - 16132.574 Da.

1   SERGLUGLNPHETHRTHRLYSLEUASNTHR
2   LEUGLUASPSERGLNGLUSERILESERSER
3   ALASERLYSTRPLEULEULEUGLNTYRARG
4   ASPALAPROLYSVALALAGLUMETTRPLYS
5   GLUTYRMETLEUARGPROSERVALASNTHR
6   ARGARGLYSLEULEUGLYLEUTYRLEUMET
7   ASNHISVALVALGLNGLNALALYSGLYGLN
8   LYSILEILEGLNPHEGLNASPSERPHEGLY
9   LYSVALALAALAGLUVALLEUGLYARGILE
10   ASNGLNGLUPHEPROARGASPLEULYSLYS
11   LYSLEUSERARGVALVALASNILELEULYS
12   GLUARGASNILEPHESERLYSGLNVALVAL
13   ASNASPILEGLUARGSERLEUALAALAALA
14   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Rtt103 (RTT) protein, [U-13C; U-15N], 0.8 mM; Potassium Phosphate 35 mM; KCl 100 mM

sample_conditions_1: ionic strength: 35 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4D HC(CC TOCSY(CO))NHsample_1isotropicsample_conditions_1
4D 13C,15N edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1
4D 13C,13C edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment

CS-Rosetta, Shen, Vernon, Baker and Bax - data analysis, refinement, structure calculation

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts