BMRB Entry 27449

Title:
Backbone 1H, 13, 15N Chemical Shifts for Repressor of Primer (Rop) Variant C38A C52V (Ala-Val)
Deposition date:
2018-04-12
Original release date:
2018-09-18
Authors:
Bowles, David; Yuan, Chunhua; Hansen, Alexandar; Stephany, Kimberly; 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:
AV_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-AVRop

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts123
15N chemical shifts63
1H chemical shifts63

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AV Rop monomer1

Entities:

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

1   GLYTHRLYSGLNGLULYSTHRALALEUASN
2   METALAARGPHEILEARGSERGLNTHRLEU
3   THRLEULEUGLULYSLEUASNGLULEUASP
4   ALAASPGLUGLNALAASPILEALAGLUSER
5   LEUHISASPHISALAASPGLULEUTYRARG
6   SERVALLEUALAARGPHEGLYASPASPGLY
7   GLUASNLEU

Samples:

sample_1: AV 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
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Ascend 700 MHz

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