BMRB Entry 27451

Title:
Backbone 1H, 15N, 13C chemical shifts for Repressor of Primer (Rop) variant IVVA
Deposition date:
2018-04-15
Original release date:
2018-09-18
Authors:
Bowles, David; Yuan, Chunhua; Lavinder, Jason; Magliery, Thomas
Citation:

Citation: Bowles, David; Yuan, Chunhua; Stephany, Kimberly; Lavinder, Jason; Hansen, Alexandar; Magliery, Thomas. "Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop"  Biomol. NMR Assignments 12, 345-350 (2018).
PubMed: 30159810

Assembly members:

Assembly members:
IVVA_Rop, polymer, 63 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pmR-IVVARop

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts62
1H chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IVVA Rop monomer1

Entities:

Entity 1, IVVA Rop monomer 63 residues - Formula weight is not available

1   METTHRLYSGLNGLULYSTHRALALEUASN
2   METALAARGPHEILEARGSERGLNVALLEU
3   THRLEULEUGLULYSLEUASNGLULEUASP
4   ALAASPGLUGLNALAASPILEALAGLUSER
5   VALHISASPHISALAASPGLULEUTYRARG
6   SERVALLEUALAARGPHEGLYASPASPGLY
7   GLUASNLEU

Samples:

sample_1: IVVA Rop, [U-100% 13C; U-100% 15N], 1.35 mM; sodium phosphate 50 mM; sodium chloride 300 mM

sample_conditions_1: ionic strength: 1.2 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_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

Software:

TOPSPIN, Bruker Biospin - collection

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing, refinement

NMR spectrometers:

  • Bruker DMX 600 MHz

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