BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17062

Title: Solution Structure of Human Plasminogen Kringle 3   PubMed: 20617841

Deposition date: 2010-07-15 Original release date: 2010-08-19

Authors: Christen, Martin; Frank, Pascal; Schaller, Johann; Llinas, Miguel

Citation: Christen, Martin; Frank, Pascal; Schaller, Johann; Llinas, Miguel. "Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape"  Biochemistry 49, 7131-7150 (2010).

Assembly members:
hPgn_rK3, polymer, 83 residues, 9505.4 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
hPgn_rK3: TYQCLKGTGENYRGNVAVTV SGHTCQHWSAQTPHTHNRTP ENFPSKNLDENYCRNPDGKR APWCHTTNSQVRWEYCKIPS CDS

Data sets:
Data typeCount
15N chemical shifts186
1H chemical shifts603

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPgn_rK31

Entities:

Entity 1, hPgn_rK3 83 residues - 9505.4 Da.

Residues -3 to -1 and 81 to 82 are outside of the kringle domain proper. Sequence follows standard kringle amino acid numbering convention

1   THRTYRGLNCYSLEULYSGLYTHRGLYGLU
2   ASNTYRARGGLYASNVALALAVALTHRVAL
3   SERGLYHISTHRCYSGLNHISTRPSERALA
4   GLNTHRPROHISTHRHISASNARGTHRPRO
5   GLUASNPHEPROSERLYSASNLEUASPGLU
6   ASNTYRCYSARGASNPROASPGLYLYSARG
7   ALAPROTRPCYSHISTHRTHRASNSERGLN
8   VALARGTRPGLUTYRCYSLYSILEPROSER
9   CYSASPSER

Samples:

sample_1: hPgn_rK3, [U-97% 15N], 1.0 mM; H2O 90%; D2O 90%; sodium azide 0.02%

Structure_determination: ionic strength: 0 M; pH*: 5.7; pressure: 1 atm; temperature: 273 K

Titrations: ionic strength: 0 M; pH*: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicStructure_determination
3D 1H-15N TOCSYsample_1isotropicStructure_determination
3D 1H-15N NOESYsample_1isotropicStructure_determination
3D HNHAsample_1isotropicStructure_determination
3D HNHBsample_1isotropicStructure_determination
2D 1H-1H COSYsample_1isotropicStructure_determination
2D 1H-1H TOCSYsample_1isotropicStructure_determination
2D 1H-1H NOESYsample_1isotropicStructure_determination
2D 1H-15N HSQCsample_1isotropicTitrations

Software:

xwinnmr v2.6, Bruker Biospin - collection

FELIX v98, Accelrys Software Inc. - processing

CcpNMR v1.0, CCPN - chemical shift assignment, data analysis, peak picking

ARIA v2.2, Linge, O, . - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17063
PDB

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