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 17973

Title: Onconase zymogen FLG variant   PubMed: 22392335

Deposition date: 2011-10-04 Original release date: 2012-03-09

Authors: Vilanova, Maria; Callis, Mariona; Laurents, Douglas; Ribo, Marc; Bruix, Marta; Serrano, Soraya

Citation: Serrano, Soraya; Callis, Mariona; Vilanova, Maria; Benito, Antoni; Laurents, Douglas; Ribo, Marc; Bruix, Marta. "(1)H, (13)C and (15)N resonance assignments of the Onconase FL-G zymogen."  Biomol. NMR Assignments 7, 13-15 (2013).

Assembly members:
onconase_FLG_variant, polymer, 120 residues, 13225.1 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_FLG_variant: RPCKYKLKKSTNKFCVTCEN QAPVHFVGVGSCGSGGSGIF LETSLSAGSDWLTFQKKHIT NTRDVDCXNIMSTNLFHCKD KNTFIYSRPEPVKAICKGII ASKNVLTTSEFYLSDCNVTS

Data sets:
Data typeCount
13C chemical shifts495
15N chemical shifts125
1H chemical shifts816

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1onconase FLG variant1

Entities:

Entity 1, onconase FLG variant 120 residues - 13225.1 Da.

It's a circular permutated variant of wt onconase. Insertion of 16 amino acids linking the wt N- and C-termini. N-and C-termini of this variant correspond to positions 73 and 72 in the wt onconase.

1   ARGPROCYSLYSTYRLYSLEULYSLYSSER
2   THRASNLYSPHECYSVALTHRCYSGLUASN
3   GLNALAPROVALHISPHEVALGLYVALGLY
4   SERCYSGLYSERGLYGLYSERGLYILEPHE
5   LEUGLUTHRSERLEUSERALAGLYSERASP
6   TRPLEUTHRPHEGLNLYSLYSHISILETHR
7   ASNTHRARGASPVALASPCYSDASASNILE
8   METSERTHRASNLEUPHEHISCYSLYSASP
9   LYSASNTHRPHEILETYRSERARGPROGLU
10   PROVALLYSALAILECYSLYSGLYILEILE
11   ALASERLYSASNVALLEUTHRTHRSERGLU
12   PHETYRLEUSERASPCYSASNVALTHRSER

Samples:

ONC_FLG_15N13C: buffer 10x 25 uL; H2O MQ 200 uL; DSS 2 uL; NaN3 2 uL; ONC_FLG, [U-100% 15N; U-13C], 2.8 mM

ONC_FLG_15N: buffer 10x 25 uL; D2O, [U-100% 2H], 200 uL; DSS 2 uL; NaN3 2 uL; ONC_FLG, [U-100% 15N], 1.8 mM

CONDITIONS_1: pH*: 5.2; pressure: 1 atm; temperature: 273 K

CONDITIONS_2: pH*: 5.2; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCONC_FLG_15N13CisotropicCONDITIONS_1
3D CBCA(CO)NHONC_FLG_15N13CisotropicCONDITIONS_1
3D CBCANHONC_FLG_15N13CisotropicCONDITIONS_1
3D HNCAONC_FLG_15N13CisotropicCONDITIONS_1
3D HN(CO)CAONC_FLG_15N13CisotropicCONDITIONS_1
3D HNCACOONC_FLG_15N13CisotropicCONDITIONS_1
3D 1H-13C NOESYONC_FLG_15N13CisotropicCONDITIONS_1
3D 1H-15N NOESYONC_FLG_15N13CisotropicCONDITIONS_1
3D HNCOONC_FLG_15N13CisotropicCONDITIONS_1
2D 1H-13C HSQCONC_FLG_15N13CisotropicCONDITIONS_1
2D 1H-13C HSQCONC_FLG_15NisotropicCONDITIONS_2
2D 1H-1H NOESYONC_FLG_15N13CisotropicCONDITIONS_1

Software:

TOPSPIN v1.3, Bruker Biospin - acquisition, processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

TALOS vTALOS +, Cornilescu, Delaglio and Bax - angular constraints

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 4173 5835 16040
PDB
GB AAL54383
SP P22069

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