BMRB Entry 30600

Title:
Solution structure of truncated peptide from PAMap53
Deposition date:
2019-04-15
Original release date:
2020-02-21
Authors:
Yuan, Y.; Castellino, F.
Citation:

Citation: Yuan, Yue; Ayinuola, Yetunde; Singh, Damini; Ayinuola, Olawole; Mayfield, Jeffrey; Quek, Adam; Whisstock, James; Law, Ruby; Lee, Shaun; Ploplis, Victoria; Castellino, Francis. "Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes"  J. Struct. Biol. 208, 18-29 (2019).
PubMed: 31301349

Assembly members:

Assembly members:
entity_1, polymer, 52 residues, 6020.605 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):

Entity Sequences (FASTA):
entity_1: GSVEKLTADAELQRLKNERH EEAELERLKSEAADHDKKEA ERKALEDKLADY

Data sets:
Data typeCount
13C chemical shifts198
15N chemical shifts50
1H chemical shifts313

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 52 residues - 6020.605 Da.

1   GLYSERVALGLULYSLEUTHRALAASPALA
2   GLULEUGLNARGLEULYSASNGLUARGHIS
3   GLUGLUALAGLULEUGLUARGLEULYSSER
4   GLUALAALAASPHISASPLYSLYSGLUALA
5   GLUARGLYSALALEUGLUASPLYSLEUALA
6   ASPTYR

Samples:

sample_1: Truncated peptide from PAMAP53, [U-99% 13C; U-99% 15N], 0.5 mM; Bis-Tris-d19, [U-2H], 20 mM; DSS 2 ug/mL; sodium azide 1 ug/mL

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TopSpin v3.5, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment, data analysis

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, 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