BMRB Entry 27596

Title:
1H, 13C, 15N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1
Deposition date:
2018-09-04
Original release date:
2019-01-10
Authors:
Bhattiprolu, Krishna; Gubens k, Nina; Wagner, Gabriel; Zechner, Ellen; Raffl, Sandra; Becker, Walter; Schrank, Evelyne; Zangger, Klaus
Citation:

Citation: Krishna, Bhattiprolu; Gubensak, Nina; Wagner, Gabriel; Zechner, Ellen; Raffl, Sandra; Becker, Walter; Schrank, Evelyne; Zangger, Klaus. "1H, 13C, 15N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1"  Biomol. NMR Assignments 13, 121-125 (2019).
PubMed: 30617945

Assembly members:

Assembly members:
R1TraIC126, polymer, 127 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: pET Z2

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts119
1H chemical shifts647

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1R1 Relaxosome1

Entities:

Entity 1, R1 Relaxosome 127 residues - Formula weight is not available

Residues 2 - 127 corresponds to residues 1630 - 1756 Methionine 1 (M1) is added during the cloning.

1   METASNSERVALGLNPROGLYALAGLYASN
2   GLYGLUPROVALTHRALAGLUVALLEUALA
3   GLNARGGLNALAGLUGLUALAILEARGARG
4   GLUTHRGLUARGARGALAASPGLUILEVAL
5   ARGLYSMETALAGLUASNLYSPROASPLEU
6   PROASPGLYLYSTHRGLULEUALAVALARG
7   ASPILEALAGLYGLNGLUARGASPARGSER
8   ALAILESERGLUARGGLUTHRALALEUPRO
9   GLUSERVALLEUARGGLUSERGLNARGGLU
10   ARGGLUALAVALARGGLUVALALAARGGLU
11   ASNLEULEUGLNGLUARGLEUGLNGLNMET
12   GLUARGASPMETVALARGASPLEUGLNLYS
13   GLULYSTHRLEUGLYGLYASP

Samples:

sample_1: R1TraIC126, [U-100% 15N], 300 uM; Na2HPO4 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 700 MHz

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