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 18916

Title: NMR solution structure of BRCT domain of yeast REV1   PubMed: 23747975

Deposition date: 2012-12-21 Original release date: 2013-01-22

Authors: Pustovalova, Yulia; Maciejewski, Mark; Korzhnev, Dmitry

Citation: Pustovalova, Yulia; Maciejewski, Mark; Korzhnev, Dmitry. "NMR mapping of PCNA interaction with translesion synthesis DNA polymerase Rev1 mediated by Rev1-BRCT domain."  J. Mol. Biol. 425, 3091-3105 (2013).

Assembly members:
entity, polymer, 94 residues, 10792.708 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):
entity: ISSQSSKIFKNCVIYINGYT KPGRLQLHEMIVLHGGKFLH YLSSKKTVTHIVASNLPLKK RIEFANYKVVSPDWIVDSVK EARLLPWQNYSLTS

Data sets:
Data typeCount
13C chemical shifts398
15N chemical shifts86
1H chemical shifts666

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BRCT domain of yeast REV11

Entities:

Entity 1, BRCT domain of yeast REV1 94 residues - 10792.708 Da.

1   ILESERSERGLNSERSERLYSILEPHELYS
2   ASNCYSVALILETYRILEASNGLYTYRTHR
3   LYSPROGLYARGLEUGLNLEUHISGLUMET
4   ILEVALLEUHISGLYGLYLYSPHELEUHIS
5   TYRLEUSERSERLYSLYSTHRVALTHRHIS
6   ILEVALALASERASNLEUPROLEULYSLYS
7   ARGILEGLUPHEALAASNTYRLYSVALVAL
8   SERPROASPTRPILEVALASPSERVALLYS
9   GLUALAARGLEULEUPROTRPGLNASNTYR
10   SERLEUTHRSER

Samples:

sample_1: Rev1-BRCT, [U-99% 13C; U-99% 15N], 70 uM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSY-arosample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

Rowland NMR Toolkit v3.1, Alan S. Stern, Jeffrey C. Hoch - processing

VNMRJ, Varian - collection

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TALOS+, Cornilescu, Delaglio and Bax, Shen, Delaglio, Cornilescu, and Bax - dihedral angle restraints

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian VNMRS 600 MHz
  • Varian VNMRS 500 MHz

Related Database Links:

PDB
DBJ GAA26649
EMBL CAA65033 CAA99674 CAY86626
GB AAA34967 AHY77615 AJP41846 AJT71268 AJT71755
REF NP_014991
SP P12689
TPG DAA11107

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