BMRB Entry 16011

Title:
NMR Spectroscopic Characterization of 13C, 15N-labeled Ribonuclease A in urea 8M
Deposition date:
2008-10-30
Original release date:
2010-10-18
Authors:
Lopez-Alonso, Jorge; Bruix, Marta; Font, Josep; Ribo, Marc; Vilanova, Maria; Morbio, Manuela; Jimenez, Maria; Rico, Manuel; Santoro, Jorge; Gonzalez, Carlos; Laurents, Douglas
Citation:

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).
PubMed: 20085318

Assembly members:

Assembly members:
ribonuclease_A, polymer, 124 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET-22b (+)

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts112
1H chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ribonuclease A1

Entities:

Entity 1, ribonuclease A 124 residues - Formula weight is not available

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: ribonuclease A, [U-98% 13C; U-98% 15N], 1.75 mM; H2O 90%; D2O 10%; urea 8 M

sample_conditions_1: pH: 2.0; 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 NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D CB-edited 1H-15N HSQCsample_1isotropicsample_conditions_1
2D CG-edited 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance US2 NMR 800 MHz

Related Database Links:

BMRB 1072 16010 16503 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
AlphaFold P61823 P61824

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