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 17172

Title: Bovine Pancreatic Ribonuclease A C-dimer   PubMed: 16415350

Deposition date: 2010-09-10 Original release date: 2010-09-13

Authors: Laurents, Douglas; Lopez, Jorge

Citation: Lopez, Jorge Pedro; Bruix, Marta; Font, Josep; Rib, Marc; Vilanova, Maria; Rico, Manuel; Gotte, Giovanni; Libonati, Massimo; Gonz lez, Carlos; Laurentr, Douglas. "Formation, structure and dissociation of the RNase S 3D domain-swapped dimer."  J. Biol. Chem. 281, 9400-9406 (2006).

Assembly members:
RNase_A_C-dimer, polymer, 124 residues, 13684 Da.

Natural source:   Common Name: Cattle   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

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

Entity Sequences (FASTA):
RNase_A_C-dimer: KETAAAKFERQHMDSSTSAA SSSNYCNQMMKSRNLTKDRC KPVNTFVHESLADVQAVCSQ KNVACKNGQTNCYQSYSTMS ITDCRETGSSKYPNCAYKTT QANKHIIVACEGNPYVPVHF DASV

Data sets:
Data typeCount
15N chemical shifts98
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNase A C-dimer, chain 11
2RNase A C-dimer, chain 21

Entities:

Entity 1, RNase A C-dimer, chain 1 124 residues - 13684 Da.

1   LYSGLUTHRALAALAALALYSPHEGLUARG
2   GLNHISMETASPSERSERTHRSERALAALA
3   SERSERSERASNTYRCYSASNGLNMETMET
4   LYSSERARGASNLEUTHRLYSASPARGCYS
5   LYSPROVALASNTHRPHEVALHISGLUSER
6   LEUALAASPVALGLNALAVALCYSSERGLN
7   LYSASNVALALACYSLYSASNGLYGLNTHR
8   ASNCYSTYRGLNSERTYRSERTHRMETSER
9   ILETHRASPCYSARGGLUTHRGLYSERSER
10   LYSTYRPROASNCYSALATYRLYSTHRTHR
11   GLNALAASNLYSHISILEILEVALALACYS
12   GLUGLYASNPROTYRVALPROVALHISPHE
13   ASPALASERVAL

Samples:

sample_1: RNase A C-dimer, [U-99% 15N], 0.08 – 1.0 mM; Na2HPO4 0.10 M; NaH2PO4 0.10 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.5 M; pH: 6.7; pressure: 1 atm; temperature: 298.0 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin, Goddard - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 1072 16010 16011 16503 16742 17099 19065 2928 385 4031 4032 443
PDB
EMBL CAA30263 CAA33801 CAB37066
GB AAA72269 AAA72757 AAB35594 AAB36134 AAI49530
PIR JC5560 NRBOB
PRF 630436A
REF NP_001014408 XP_005211519 XP_005901936 XP_010837737
SP P61823 P61824
TPE CDG32088
TPG DAA25470
AlphaFold P61823 P61824

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