BMRB Entry 50115

Title:
Backbone 13C, and 15N Chemical Shift Assignments for ChiZ N-terminal Domain
Deposition date:
2019-12-06
Original release date:
2020-06-23
Authors:
Escobar, Cristian; Cross, Timothy
Citation:

Citation: Hicks, Alan; Escobar, Cristian; Cross, Timothy; Zhou, Huan-Xiang. "Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ"  Biomolecules 10, 946-946 (2020).

Assembly members:

Assembly members:
entity_1, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTBSG1

Experimental source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTBSG1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts52
1H chemical shifts52
H exchange rates50
T1 relaxation values50
T2 relaxation values50
heteronuclear NOE values52

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain1

Entities:

Entity 1, N-terminal domain 67 residues - Formula weight is not available

ChiZ residues 1 to 64 plus first 3 residues (SNA) left from TEV protease cleavage site. Residues 1-64 correspond to the cytoplasmatic soluble domain of ChiZ membrane protein.

1   SERASNALAMETTHRPROVALARGPROPRO
2   HISTHRPROASPPROLEUASNLEUARGGLY
3   PROLEUASPGLYPROARGTRPARGARGALA
4   GLUPROALAGLNSERARGARGPROGLYARG
5   SERARGPROGLYGLYALAPROLEUARGTYR
6   HISARGTHRGLYVALGLYMETSERARGTHR
7   GLYHISGLYSERARGPROVAL

Samples:

sample_1: entity_1, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; DSS 50 uM; D2O 10 % v/v; sodium chloride 25 mM

sample_conditions_1: ionic strength: 45 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
HN(CA)COsample_1isotropicsample_conditions_1
15N-(1H) NOEsample_1isotropicsample_conditions_1
Het. Nuc. T1 relaxationsample_1isotropicsample_conditions_1
Het. Nuc. T2 relaxationsample_1isotropicsample_conditions_1
CLEANEX-PM (15N-HSQC)sample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

CcpNMR v2.4.2, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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