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 16503

Title: Ribonuclease A in 40% acetic acid and 8M urea pH 2   PubMed: 20085318

Authors: L pez Alonso, Jorge; Bruix, Marta; Laurents, Douglas

Citation: Lopez-Alonso, Jorge Pedro; Bruix, Marta; Font, Josep; Ribo, Marc; Vilanova, Maria; Jimenez, Maria Angeles; Santoro, Jorge; Gonzalez, Carlos; Laurents, Douglas. "NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping."  J. Am. Chem. Soc. 132, 1621-1630 (2010).

Assembly members:
RNase_A, polymer, 124 residues, 13684 Da.

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

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

Entity Sequences (FASTA):
RNase_A: KETAAAKFERQHMDSSTSAA SSSNYCNQMMKSRNLTKDRC KPVNTFVHESLADVQAVCSQ KNVACKNGQTNCYQSYSTMS ITDCRETGSSKYPNCAYKTT QANKHIIVACEGNPYVPVHF DASV

Data sets:
Data typeCount
13C chemical shifts602
15N chemical shifts229
1H chemical shifts351

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNase A1

Entities:

Entity 1, RNase A 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, [U-13C], 1.7 mM; acetic acid 40%; H2O 50%; D2O 10%

sample_2: RNase A, [U-100% 13C; U-100% 15N], 1.7 mM; D2O 10%; urea 8 M

sample_conditions_1: ionic strength: 0.024 M; pH: 2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.005 M; pH: 2.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
1H-15N HSQC side chain filteredsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 1072 16010 16011 16742 17099 17172 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