BMRB Entry 30390

Title:
Solution structure of KTI55
Deposition date:
2017-12-24
Original release date:
2019-01-11
Authors:
Castellino, F.; Qiu, C.; Yuan, Y.
Citation:

Citation: Qiu, Cunjia; Yuan, Yue; Zajicek, Jaroslav; Liang, Zhong; Balsara, Rashna; Brito-Robionson, Teresa; Lee, Shaun; Ploplis, Victoria; Castellino, Francis. "Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization"  J. Struct. Biol. 204, 151-164 (2018).
PubMed: 30071314

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, 6799.461 Da.

Natural source:

Natural source:   Common Name: Streptococcus pyogenes   Taxonomy ID: 1314   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pyogenes

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli DH5[alpha]   Vector: pET15b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts55
1H chemical shifts354

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 57 residues - 6799.461 Da.

1   GLYSERLYSTHRILEGLNGLULYSGLUGLN
2   GLULEULYSASNLEULYSASPASNVALGLU
3   LEUGLUARGLEULYSASNGLUARGHISASP
4   HISASPGLUGLUALAGLUARGLYSALALEU
5   GLUASPLYSLEUALAASPLYSGLNGLUHIS
6   LEUASPGLYALALEUARGTYR

Samples:

sample_1: BisTris-d19, [U-99% 2H], 20 mM; DSS 1 mM; sodium azide 1 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_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 NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker AvanceII 800 MHz

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