BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30599

Title: Solution structure of VEK50RH1/AA

Deposition date: 2019-04-15 Original release date: 2020-02-21

Authors: Yuan, Y.; Castellino, F.

Citation: Yuan, Y.; Ploplis, V.; Lee, S.; Castellino, F.. "Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcal pyogenes cells"  . ., .-..

Assembly members:
entity_1, polymer, 52 residues, 6020.606 Da.

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

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

Entity Sequences (FASTA):
entity_1: GSVEKLTADAELQRLKNEAA EEAELERLKSERHDHDKKEA ERKALEDKLADY

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts49
1H chemical shifts299

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 - 6020.606 Da.

1   GLYSERVALGLULYSLEUTHRALAASPALA
2   GLULEUGLNARGLEULYSASNGLUALAALA
3   GLUGLUALAGLULEUGLUARGLEULYSSER
4   GLUARGHISASPHISASPLYSLYSGLUALA
5   GLUARGLYSALALEUGLUASPLYSLEUALA
6   ASPTYR

Samples:

sample_1: VEK50RH1/AA, [U-99% 13C; U-99% 15N], 0.5 mM; DSS 2 ug/mL; DTT 1 ug/mL; Bis-Tris-d19, [U-2H], 20 mM

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 HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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