BMRB Entry 34996

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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/BMR34996
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Staphylokinase SY155
Deposition date:
2025-05-21
Original release date:
2026-04-15
Authors:
Legrand, A.; Kaderavek, P.; Zidek, L.; Marek, M.; Prokop, Z.; Damborsky, J.
Citation:

Citation: Legrand, A.; Kasiarova, L.; Verma, N.; Mican, J.; Strunga, A.; Iglesias-Planas, J.; Kucera, J.; Henek, T.; Vanacek, P.; Kaderavek, P.; Zidek, L.; Damborsky, J.; Mazurenko, S.; Bednar, D.; Hernychova, L.; Prokop, Z.; Marek, M.. "Dynamics of non-immunogenic staphylokinase thrombolytics"  .

Assembly members:

Assembly members:
entity_1, polymer, 136 residues, 15252.247 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSSFDKGKYKKGDDASYFEP TGPYLMVNVTGVDSAGNELL SPHYVEFPIKPGTTLTKEKI EYYVQWALDATAYREFRVVE LAPAAKIEVAYYDKNKKKDE SKSFPITAAGFVVPDLSEHI KNPGFNLITTVVIERK

Data sets:
Data typeCount
13C chemical shifts599
15N chemical shifts133
1H chemical shifts983

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 136 residues - 15252.247 Da.

1   SERSERSERPHEASPLYSGLYLYSTYRLYS
2   LYSGLYASPASPALASERTYRPHEGLUPRO
3   THRGLYPROTYRLEUMETVALASNVALTHR
4   GLYVALASPSERALAGLYASNGLULEULEU
5   SERPROHISTYRVALGLUPHEPROILELYS
6   PROGLYTHRTHRLEUTHRLYSGLULYSILE
7   GLUTYRTYRVALGLNTRPALALEUASPALA
8   THRALATYRARGGLUPHEARGVALVALGLU
9   LEUALAPROALAALALYSILEGLUVALALA
10   TYRTYRASPLYSASNLYSLYSLYSASPGLU
11   SERLYSSERPHEPROILETHRALAALAGLY
12   PHEVALVALPROASPLEUSERGLUHISILE
13   LYSASNPROGLYPHEASNLEUILETHRTHR
14   VALVALILEGLUARGLYS

Samples:

sample_1: Staphylokinase SY155, [U-13C; U-15N], 466 uM; sodium phosphate, none, 50 mM; NaCl, none, 100 mM; EDTA, none, 0.5 mM; DTT, none, 1 mM; sodium azide, none, 0.04%

sample_conditions_1: ionic strength: 150 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
CBCACONHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
CBCANHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection, processing

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - chemical shift assignment, peak picking, structure calculation

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

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