BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 4371

Title: Sequence-specific 1H, 13C and 15N Resonance Assignments of Recombinant Onconase/P-30 Protein

Deposition date: 1999-07-20 Original release date: 2003-06-16

Authors: Gorbatyuk, Vitaliy; Chen, Yi-Cheng; Wu, Yung-Jean; Youle, Richard; Huang, Tai-huang

Citation: Gorbatyuk, Vitaliy; Chen, Yi-Cheng; Wu, Yung-Jean; Youle, Richard; Huang, Tai-huang. "Sequence-specific 1H, 13C and 15N Resonance Assignments of Recombinant Onconase/P-30 Protein"  J. Biomol. NMR 15, 343-344 (1999).

Assembly members:
Recombinant Onconase/ranpirnase, polymer, 105 residues, 11958 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   Vector: pET-11d

Entity Sequences (FASTA):
Recombinant Onconase/ranpirnase: MQDWLTFQKKHITNTRDVDC DNILSTNLFHCKDKNTFIYS RPEPVKAICKGIIASKNVLT TSEFYLSDCNVTSRPCKYKL KKSTNKFCVTCENQAPVHFV GVGSC

Data sets:
Data typeCount
13C chemical shifts470
15N chemical shifts223
1H chemical shifts825

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1(M-1,Q1,M23L)rOnc1

Entities:

Entity 1, (M-1,Q1,M23L)rOnc 105 residues - 11958 Da.

1   METGLNASPTRPLEUTHRPHEGLNLYSLYS
2   HISILETHRASNTHRARGASPVALASPCYS
3   ASPASNILELEUSERTHRASNLEUPHEHIS
4   CYSLYSASPLYSASNTHRPHEILETYRSER
5   ARGPROGLUPROVALLYSALAILECYSLYS
6   GLYILEILEALASERLYSASNVALLEUTHR
7   THRSERGLUPHETYRLEUSERASPCYSASN
8   VALTHRSERARGPROCYSLYSTYRLYSLEU
9   LYSLYSSERTHRASNLYSPHECYSVALTHR
10   CYSGLUASNGLNALAPROVALHISPHEVAL
11   GLYVALGLYSERCYS

Samples:

sample_1: Recombinant Onconase/ranpirnase, [U-15N; U-13C], 1.5 mM

sample_conditions_set_1: pH*: 4.1; temperature: 310 K

sample_conditions_set_2: pH*: 7.0; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1not availablenot available
2D 13C CT-HSQCsample_1not availablenot available
3D CBCANHsample_1not availablenot available
3D CBCA(CO)NHsample_1not availablenot available
3D HBHA(CO)NHsample_1not availablenot available
3D HNCOsample_1not availablenot available
3D HN(CA)COsample_1not availablenot available
3D 15N-res. [1H,1H]-TOCSY (mixing time: 60.4 ms)sample_1not availablenot available
3D HCCH-COSYsample_1not availablenot available
3D HCCH-TOCSY (mixing time: 24.8 ms)sample_1not availablenot available
3D 15N-res. NOESY-HSQC (mixing time 100 ms)sample_1not availablenot available
3D 13C-res. NOESY-HSQC (mixing time 100 ms)sample_1not availablenot available
2D 13C-filtered NOESY (mixing time 100 ms)sample_1not availablenot available
2D 13C-filtered TOCSYsample_1not availablenot available

Software:

XWINNMR - data processing

AURELIA - assignment

Sparky - assignment

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16040
PDB
GB AAL54383
SP P22069
AlphaFold P22069

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