BMRB Entry 50409

Title:
SoRNHI 15N-1H Backbone Chemical Shifts
Deposition date:
2020-07-24
Original release date:
2020-07-30
Authors:
Martin, James; Robustelli, Paul; Palmer, Arthur
Citation:

Citation: Martin, James; Robustelli, Paul; Palmer, Arthur. "Quantifying the Relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues"  Biochemistry 59, 3201-3205 (2020).
PubMed: 32813972

Assembly members:

Assembly members:
entity_1, polymer, 158 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Shewanella oneidensis   Taxonomy ID: 70863   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Shewanella oneidensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-25b(+)

Data sets:
Data typeCount
15N chemical shifts151
1H chemical shifts151

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SoRNHI1

Entities:

Entity 1, SoRNHI 158 residues - Formula weight is not available

1   METTHRGLULEULYSLEUILEHISILEPHE
2   THRASPGLYSERCYSLEUGLYASNPROGLY
3   PROGLYGLYTYRGLYILEVALMETASNTYR
4   LYSGLYHISTHRLYSGLUMETSERASPGLY
5   PHESERLEUTHRTHRASNASNARGMETGLU
6   LEULEUALAPROILEVALALALEUGLUALA
7   LEULYSGLUPROCYSLYSILEILELEUTHR
8   SERASPSERGLNTYRMETARGGLNGLYILE
9   METTHRTRPILEHISGLYTRPLYSLYSLYS
10   GLYTRPMETTHRSERASNARGTHRPROVAL
11   LYSASNVALASPLEUTRPLYSARGLEUASP
12   LYSALAALAGLNLEUHISGLNILEASPTRP
13   ARGTRPVALLYSGLYHISALAGLYHISALA
14   GLUASNGLUARGCYSASPGLNLEUALAARG
15   ALAALAALAGLUALAASNPROTHRGLNILE
16   ASPTHRGLYTYRGLNALAGLUSER

Samples:

sample_1: S. oneidensis Ribonuclease HI, [U-100% 13C; U-100% 15N], 325 uM; deuterated sodium acetate 50 mM; sodium chloride 50 mM; sodium azide 0.02 % (w/v); DTT 1 mM; DSS 3 mM

sample_conditions_1: ionic strength: 0.050 M; pH: 5.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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