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 16040

Title: Solution structure of onconase C87A/C104A   PubMed: 19655705

Authors: Weininger, Ulrich; Schulenburg, Cindy; Arnold, Ulrich; Ulbrich-Hofmann, Renate; Balbach, Jochen

Citation: Schulenburg, Cindy; Low, Christian; Weininger, Ulrich; Mrestani-Klaus, Carmen; Hofmann, Hagen; Balbach, Jochen; Ulbrich-Hofmann, Renate; Arnold, Ulrich. "The folding pathway of onconase is directed by a conserved intermediate"  Biochemistry 48, 8449-8457 (2009).

Assembly members:
onconase C87A/C104A, polymer, 104 residues, 11781.603 Da.

Natural source:   Common Name: northern leopard frog   Taxonomy ID: 8404   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: rana pipiens

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

Entity Sequences (FASTA):
onconase C87A/C104A: XDWLTFQKKHITNTRDVDCD NIMSTNLFHCKDKNTFIYSR PEPVKAICKGIIASKNVLTT SEFYLSDCNVTSRPCKYKLK KSTNKFAVTCENQAPVHFVG VGSA

Data sets:
Data typeCount
15N chemical shifts109
1H chemical shifts744

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1onconase C87A/C104A1

Entities:

Entity 1, onconase C87A/C104A 104 residues - 11781.603 Da.

1   PCAASPTRPLEUTHRPHEGLNLYSLYSHIS
2   ILETHRASNTHRARGASPVALASPCYSASP
3   ASNILEMETSERTHRASNLEUPHEHISCYS
4   LYSASPLYSASNTHRPHEILETYRSERARG
5   PROGLUPROVALLYSALAILECYSLYSGLY
6   ILEILEALASERLYSASNVALLEUTHRTHR
7   SERGLUPHETYRLEUSERASPCYSASNVAL
8   THRSERARGPROCYSLYSTYRLYSLEULYS
9   LYSSERTHRASNLYSPHEALAVALTHRCYS
10   GLUASNGLNALAPROVALHISPHEVALGLY
11   VALGLYSERALA

Samples:

sample_1: entity, [U-15N], 1.0 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 4371
PDB
GB AAL54383
SP P22069