BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30043

Title: NMR solution structure of Mayaro virus macro domain

Deposition date: 2016-03-10 Original release date: 2017-12-13

Authors: Melekis, E.; Tsika, A.; Bentrop, D.; Papageorgiou, N.; Coutard, B.; Spyroulias, G.

Citation: Melekis, E.; Tsika, A.; Bentrop, D.; Papageorgiou, N.; Coutard, B.; Spyroulias, G.; Melekis, E.; Tsika, A.; Lichiere, J.; Chasapis, C.; Margiolaki, I.; Papageorgiou, N.; Coutard, B.; Bentrop, D.; Spyroulias, G.; Makrynitsa, G.; Ntonti, D.; Marousis, K.; Tsika, A.; Lichiere, J.; Papageorgiou, N.; Coutard, B.; Bentrop, D.; Spyroulias, G.; Papageorgiou, N.; Watier, Y.; Saunders, L.; Coutard, B.; Lantez, V.; Gould, E.; Fitch, A.; Wright, J.; Canard, B.; Margiolaki, I.. "NMR solution structure of Mayaro virus macro domain"  . ., .-..

Assembly members:
entity_1, polymer, 166 residues, 18147.494 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MAPAYTVKRADIATAIEDAV VNAANHRGQVGDGVCRAVAR KWPQAFRNAATPVGTAKTVK CDETYIIHAVGPNFNNTSEA EGDRDLAAAYRAVAAEINRL SISSVAIPLLSTGIFSAGKD RVHQSLSHLLAAMDTTEARV TIYCRDKTWEQKIKTVLQNR HHHHHH

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts136
1H chemical shifts917

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 166 residues - 18147.494 Da.

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

Samples:

sample_1: Mayaro virus' macro domain 0.4 mM

sample_2: Mayaro virus' macro domain, [U-99% 15N], 0.4 mM

sample_3: Mayaro virus' macro domain, [U-99% 13C; U-99% 15N], 0.4 mM

sample_4: Mayaro virus' macro domain, [U-15N]-Ala-Leu-Val, 0.4 mM

sample_5: Mayaro virus' macro domain, [U-14N]-Arg, 0.4 mM

sample_6: Mayaro virus' macro domain, [U-14N]-Asn-Cys, 0.4 mM

sample_7: Mayaro virus' macro domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM

sample_8: Mayaro virus' macro domain 0.5 mM

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

sample_conditions_2: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
3D HNCACBsample_7isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
2D 1H-15N HSQC TROSYsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v3.3, Bruker Biospin - collection, processing

TOPSPIN v3.2, Bruker Biospin - collection, processing

CARA v1.5.5, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - peak picking

DYANA, Guntert, Braun and Wuthrich - structure calculation

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Bruker Avance 600 MHz
  • Bruker Bruker Avance III High-Definition four-channel 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts