BMRB Entry 19927

Title:
NMR study of non-structural proteins - 1H, 13C, 15N resonance assignment of macro domain from Mayaro virus (MAYV)
Deposition date:
2014-04-21
Original release date:
2019-01-03
Authors:
Melekis, Stathis; Chasapis, Christos; Tsika, Aikaterini; Bentrop, Detlef; Spyroulias, Georgios
Citation:

Citation: Melekis, Stahis; Tsika, Aikaterini; Lichiere, Julie; Chasapis, Christos; Margiolaki, Irene; Papageorgiou, Nicolas; Coutard, Bruno; Bentrop, Detlef; Spyroulias, Georgios. "NMR study of non-structural proteins - part I: 1H, 13C, 15N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV)"  Biomol. NMR Assignments 9, 191-195 (2015).

Assembly members:

Assembly members:
Mayaro_macro_domain, polymer, 159 residues, 17163.4 Da.

Natural source:

Natural source:   Common Name: Mayaro virus   Taxonomy ID: 374990   Superkingdom: Viruses   Kingdom: not available   Genus/species: Alphavirus Mayaro

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDesT 14

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts136
1H chemical shifts921

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mayaro macro domain1

Entities:

Entity 1, Mayaro macro domain 159 residues - 17163.4 Da.

1   ALAPROALATYRTHRVALLYSARGALAASP
2   ILEALATHRALAILEGLUASPALAVALVAL
3   ASNALAALAASNHISARGGLYGLNVALGLY
4   ASPGLYVALCYSARGALAVALALAARGLYS
5   TRPPROGLNALAPHEARGASNALAALATHR
6   PROVALGLYTHRALALYSTHRVALLYSCYS
7   ASPGLUTHRTYRILEILEHISALAVALGLY
8   PROASNPHEASNASNTHRSERGLUALAGLU
9   GLYASPARGASPLEUALAALAALATYRARG
10   ALAVALALAALAGLUILEASNARGLEUSER
11   ILESERSERVALALAILEPROLEULEUSER
12   THRGLYILEPHESERALAGLYLYSASPARG
13   VALHISGLNSERLEUSERHISLEULEUALA
14   ALAMETASPTHRTHRGLUALAARGVALTHR
15   ILETYRCYSARGASPLYSTHRTRPGLUGLN
16   LYSILELYSTHRVALLEUGLNASNARG

Samples:

sample_1: Mayaro macro domain, [U-99% 15N], 0.4 mM; H20 90%; D20 10%

sample_2: Mayaro macro domain, [U-98% 13C; U-98% 15N], 0.4 mM; H20 90%; D20 10%

sample_3-5: Mayaro macro domain, [U-99% 15N], 0.4 mM; H20 90%; D20 10%

sample_6: Mayaro macro domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 30 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3-5isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_6isotropicsample_conditions_1
3D CBCA(CO)NHsample_6isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance-III 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q8QZ73
AlphaFold Q8QHM4

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