BMRB Entry 30271

Title:
Solution structure of VKK38 bound to plasminogen kringle 2
Deposition date:
2017-03-10
Original release date:
2017-07-20
Authors:
Yuan, Y.; Castellino, F.
Citation:

Citation: Yuan, Yue; Zajicek, Jaroslav; Qiu, Cunjia; Chandrahas, Vishwanatha; Lee, Shaun; Ploplis, Victoria; Castellino, Francis. "Conformationally organized lysine isosteres in Streptococcus pyogenes M protein mediate direct high-affinity binding to human plasminogen"  J. Biol. Chem. 292, 15016-15027 (2017).
PubMed: 28724633

Assembly members:

Assembly members:
M protein, polymer, 40 residues, 4892.360 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
M protein: GSVKKLNDEVALERLKNERH VHDEEVELERLKNERHDHDY

Data sets:
Data typeCount
13C chemical shifts133
15N chemical shifts37
1H chemical shifts170

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 40 residues - 4892.360 Da.

1   GLYSERVALLYSLYSLEUASNASPGLUVAL
2   ALALEUGLUARGLEULYSASNGLUARGHIS
3   VALHISASPGLUGLUVALGLULEUGLUARG
4   LEULYSASNGLUARGHISASPHISASPTYR

Samples:

sample_1: BisTris-d19, [U-100% 2H], 20 mM; DSS 0.2 mM; EDTA 2 mM; Kringle2 2.5 mM; VKK38, [U-13C; U-15N], 1.0 mM; sodium azide 3 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 C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 15N HSQC-NOESYsample_1isotropicsample_conditions_1

Software:

TALOS-N, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - chemical shift assignment, peak picking

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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