BMRB Entry 50407

Title:
V98A EcRNHI* (Cys-free) 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, 155 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Data sets:
Data typeCount
15N chemical shifts152
1H chemical shifts152

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1V98A EcRNHI*1

Entities:

Entity 1, V98A EcRNHI* 155 residues - Formula weight is not available

1   METLEULYSGLNVALGLUILEPHETHRASP
2   GLYSERALALEUGLYASNPROGLYPROGLY
3   GLYTYRGLYALAILELEUARGTYRARGGLY
4   ARGGLULYSTHRPHESERALAGLYTYRTHR
5   ARGTHRTHRASNASNARGMETGLULEUMET
6   ALAALAILEVALALALEUGLUALALEULYS
7   GLUHISALAGLUVALILELEUSERTHRASP
8   SERGLNTYRVALARGGLNGLYILETHRGLN
9   TRPILEHISASNTRPLYSLYSARGGLYTRP
10   LYSTHRALAASPLYSLYSPROALALYSASN
11   VALASPLEUTRPGLNARGLEUASPALAALA
12   LEUGLYGLNHISGLNILELYSTRPGLUTRP
13   VALLYSGLYHISALAGLYHISPROGLUASN
14   GLUARGALAASPGLULEUALAARGALAALA
15   ALAMETASNPROTHRLEUGLUASPTHRGLY
16   TYRGLNVALGLUVAL

Samples:

sample_1: V98A E. coli 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); DSS 3 mM

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

Experiments:

NameSampleSample stateSample conditions
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
  • Bruker Avance 900 MHz

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