BMRB Entry 27612

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27612

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Title:
NMR study of non-structural proteins - 1H, 13C, 15N resonance assignment of macro domain from Mayaro virus (MAYV) in complex with ADP-ribose
Deposition date:
2018-09-14
Original release date:
2019-05-24
Authors:
Tsika, Aikaterini; Melekis, Efstathios; Coutard, Bruno; Bentrop, Detlef; Spyroulias, Georgios
Citation:

Citation: Tsika, Aikaterini; Melekis, Efstathios; Tsatsouli, Sofia-Antigoni; Papageorgiou, Nicolas; Mate, Maria; Canard, Bruno; Coutard, Bruno; Bentrop, Detlef; Spyroulias, Georgios. "Deciphering the Nucleotide and RNA Binding Selectivity of the Mayaro Virus Macro Domain."  J. Mol. Biol. 431, 2283-2297 (2019).
PubMed: 30998933

Assembly members:

Assembly members:
MAYV_macro_domain, polymer, 166 residues, 18117.46 Da.
entity_APR, non-polymer, 559.316 Da.

Natural source:

Natural source:   Common Name: Mayaro Virus   Taxonomy ID: 59301   Superkingdom: Viruses   Kingdom: not available   Genus/species: Mayaro Virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDest14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MAYV_macro_domain: MAPAYTVKRADIATAIEDAV VNAANHRGQVGDGVCRAVAR KWPQAFRNAATPVGTAKTVK CDETYIIHAVGPNFNNTSEA EGDRDLAAAYRAVAAEINRL SISSVAIPLLSTGIFSAGKD RVHQSLSHLLAAMDTTEARV TIYCRDKTWEQKIKTVLQNR HHHHHH

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts140
1H chemical shifts942

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
111
222

Entities:

Entity 1, 1 166 residues - 18117.46 Da.

Residue 1 represents a methionine derived from the start codon in the DNA sequence. Residues 161-166 represent a non-native affinity tag.

1   METALAPROALATYRTHRVALLYSARGALA
2   ASPILEALATHRALAILEGLUASPALAVAL
3   VALASNALAALAASNHISARGGLYGLNVAL
4   GLYASPGLYVALCYSARGALAVALALAARG
5   LYSTRPPROGLNALAPHEARGASNALAALA
6   THRPROVALGLYTHRALALYSTHRVALLYS
7   CYSASPGLUTHRTYRILEILEHISALAVAL
8   GLYPROASNPHEASNASNTHRSERGLUALA
9   GLUGLYASPARGASPLEUALAALAALATYR
10   ARGALAVALALAALAGLUILEASNARGLEU
11   SERILESERSERVALALAILEPROLEULEU
12   SERTHRGLYILEPHESERALAGLYLYSASP
13   ARGVALHISGLNSERLEUSERHISLEULEU
14   ALAALAMETASPTHRTHRGLUALAARGVAL
15   THRILETYRCYSARGASPLYSTHRTRPGLU
16   GLNLYSILELYSTHRVALLEUGLNASNARG
17   HISHISHISHISHISHIS

Entity 2, 2 - C15 H23 N5 O14 P2 - 559.316 Da.

1   APR

Samples:

sample_1: MAYV MD, [U-99% 15N], 0.4 mM; ADP-ribose 1.6 mM; HEPES 10 mM; NaCl 20 mM

sample_2: MAYV MD, [U-99% 13C; U-99% 15N], 0.6 mM; ADP-ribose 1.2 mM; HEPES 10 mM; NaCl 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance HD- III HD 700 MHz

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