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 5787

Title: 1H, 13C and 15N resonance assignments and secondary structure of the cytotoxic protein RNase 3 from oocytes of bullfrog Rana catesbeiana

Deposition date: 2003-04-29 Original release date: 2003-09-05

Authors: Lou, Yuan-Chao; Pan, Yun-Ru; Ho, Yi-Hsuan; Liao, You-Di; Chen, Chinpan

Citation: Lou, Yuan-Chao; Pan, Yun-Ru; Ho, Yi-Hsuan; Liao, You-Di; Chen, Chinpan. "Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of the cytotoxic protein RNase 3 from oocytes of bullfrog Rana catesbeiana"  J. Biomol. NMR 27, 289-290 (2003).

Assembly members:
RC-RNase 3, polymer, 105 residues, 11876 Da.
PCA, non-polymer, 129.114 Da.

Natural source:   Common Name: bullfrog   Taxonomy ID: 8400   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rana catesbeiana

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11d

Entity Sequences (FASTA):
RC-RNase 3: XDWETFQKKHLTDTKKVKCD VEMAKALFDCKKTNTFIYAL PGRVKALCKNIRDNTDVLSR DAFLLPQCDRIKLPCHYKLS SSTNTICITCVNQLPIHFAG VGSCP

Data sets:
Data typeCount
1H chemical shifts754
13C chemical shifts484
15N chemical shifts108

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RC-RNase 31

Entities:

Entity 1, RC-RNase 3 105 residues - 11876 Da.

1   PCAASPTRPGLUTHRPHEGLNLYSLYSHIS
2   LEUTHRASPTHRLYSLYSVALLYSCYSASP
3   VALGLUMETALALYSALALEUPHEASPCYS
4   LYSLYSTHRASNTHRPHEILETYRALALEU
5   PROGLYARGVALLYSALALEUCYSLYSASN
6   ILEARGASPASNTHRASPVALLEUSERARG
7   ASPALAPHELEULEUPROGLNCYSASPARG
8   ILELYSLEUPROCYSHISTYRLYSLEUSER
9   SERSERTHRASNTHRILECYSILETHRCYS
10   VALASNGLNLEUPROILEHISPHEALAGLY
11   VALGLYSERCYSPRO

Samples:

sample_1: RC-RNase 3, [U-13C; U-15N], 1.0 mM

sample_2: RC-RNase 3 1.5 mM

sample_condition: pH: 3.5; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D TOCSYnot availablenot availablesample_condition
2D DQF-COSYnot availablenot availablesample_condition
2D NOESYnot availablenot availablesample_condition
2D 1H-13C HSQCnot availablenot availablesample_condition
2D 1H-15N HSQCnot availablenot availablesample_condition
3D HNCACBnot availablenot availablesample_condition
3D CBCA(CO)NHnot availablenot availablesample_condition
3D HNCOnot availablenot availablesample_condition
3D HN(CA)COnot availablenot availablesample_condition
3D 15N NOESY-HSQCnot availablenot availablesample_condition
3D 15N TOCSY-HSQCnot availablenot availablesample_condition
3D C(CO)NHnot availablenot availablesample_condition
3D HC(CO)NHnot availablenot availablesample_condition
3D HCCH-TOCSYnot availablenot availablesample_condition

Software:

Xwinnmr v2.6 - data processing

Aurelia v2.1.3 - assignment

Nmrpipe v2.1 - data processing

Nmrview v5.0 - assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
GenBank AAG31440.2

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