BMRB Entry 30687

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30687
MolProbity Validation Chart

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Title:
Solution structure of KTI55-Kringle 2 complex
Deposition date:
2019-11-14
Original release date:
2020-12-04
Authors:
Qiu, C.; Yuan, Y.; Castellino, F.
Citation:

Citation: Qiu, C.; Yuan, Y.; Ploplis, V.; Castellino, F.. "Structural evolution of the A-domain in plasminogen-binding Group A streptococcal M-protein reflects improved adaptability of the pathogen to the host"  .

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, 10166.340 Da.
entity_2, polymer, 57 residues, 6799.461 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Komagataella pastoris

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: YVEFSEECMHGSGENYDGKI SKTMSGLECQAWDSQSPHAH GYIPSKFPNKNLKKNYCRNP DRDLRPWCFTTDPNKRWEYC DIPRCAA
entity_2: GSKTIQEKEQELKNLKDNVE LERLKNERHDHDEEAERKAL EDKLADKQEHLDGALRY

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts54
1H chemical shifts305

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 87 residues - 10166.340 Da.

1   TYRVALGLUPHESERGLUGLUCYSMETHIS
2   GLYSERGLYGLUASNTYRASPGLYLYSILE
3   SERLYSTHRMETSERGLYLEUGLUCYSGLN
4   ALATRPASPSERGLNSERPROHISALAHIS
5   GLYTYRILEPROSERLYSPHEPROASNLYS
6   ASNLEULYSLYSASNTYRCYSARGASNPRO
7   ASPARGASPLEUARGPROTRPCYSPHETHR
8   THRASPPROASNLYSARGTRPGLUTYRCYS
9   ASPILEPROARGCYSALAALA

Entity 2, entity_2 57 residues - 6799.461 Da.

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

Samples:

sample_1: KTI55, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; Kringle 2 1.2 ± 0.1 mM; Bis-Tris-d19, [U-2H], 20 mM; DSS 2 ug/mL; sodium azide 2 ug/mL

sample_2: KTI55 1.2 ± 0.1 mM; Kringle 2, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; Bis-Tris-d19, [U-2H], 20 mM; DSS 2 ug/mL; sodium azide 2 ug/mL

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

Experiments:

NameSampleSample stateSample conditions
2D TROSY-[1H-15N] HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-C(CO)NHsample_1isotropicsample_conditions_1
3D TROSY-HBHA(CBCA)NHsample_1isotropicsample_conditions_1
3D TROSY-H(CCO)NHsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
3D NOESYsample_1isotropicsample_conditions_1
2D IPAPsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D NOESYsample_2isotropicsample_conditions_1
2D IPAPsample_2anisotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection, processing

Sparky, Goddard - data analysis

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

HADDOCK, Bonvin - refinement

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