BMRB Entry 30298

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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/BMR30298
MolProbity Validation Chart

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Title:
Solution NMR structure of the BRCT domain of S. cerevisiae Rev1
Deposition date:
2017-05-23
Original release date:
2018-01-25
Authors:
Xu, C.; Cui, G.; Botuyan, M.; Mer, G.
Citation:

Citation: Xu, C.; Cui, G.; Botuyan, M.; Mer, G.. "Solution NMR structure of the BRCT domain of S. cerevisiae Rev1"  .

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 10703.555 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   Vector: pTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMSSKIFKNCVIYINGYTK PGRLQLHEMIVLHGGKFLHY LSSKKTVTHIVASNLPLKKR IEFANYKVVSPDWIVDSVKE ARLLPWQNYSLTS

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts93
1H chemical shifts624

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 93 residues - 10703.555 Da.

1   GLYHISMETSERSERLYSILEPHELYSASN
2   CYSVALILETYRILEASNGLYTYRTHRLYS
3   PROGLYARGLEUGLNLEUHISGLUMETILE
4   VALLEUHISGLYGLYLYSPHELEUHISTYR
5   LEUSERSERLYSLYSTHRVALTHRHISILE
6   VALALASERASNLEUPROLEULYSLYSARG
7   ILEGLUPHEALAASNTYRLYSVALVALSER
8   PROASPTRPILEVALASPSERVALLYSGLU
9   ALAARGLEULEUPROTRPGLNASNTYRSER
10   LEUTHRSER

Samples:

sample_1: NaCl 50 mM; Rev1-BRCT, [U-100% 15N], 1 mM; Sodium phosphate buffer 50 mM

sample_2: NaCl 50 mM; Rev1-BRCT, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate buffer 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - processing

SPARKY, Goddard - chemical shift assignment, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • 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