BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27158

Title: NMR study of non-structural proteins part III: 1H, 13C, 15N resonance assignment of macro domain from Chikungunya virus (CHIKV)   PubMed: 28875416

Authors: Lykouras, Michail; Tsika, Aikaterini; Lichiere, Julie; Papageorgiou, Nicolas; Coutard, Bruno; Bentrop, Detlef; Spyroulias, Georgios

Citation: Lykouras, Michail; Tsika, Aikaterini; Lichiere, Julie; Papageorgiou, Nicolas; Coutard, Bruno; Bentrop, Detlef; Spyroulias, Georgios. "NMR study of non-structural proteins-part III: 1H, 13C, 15N backbone and side-chain resonance assignment of macro domain from Chikungunya virus (CHIKV)"  Biomol. NMR Assignments ., .-. (2017).

Assembly members:
CHIKV_macro_domain, polymer, 168 residues, 18605.07 Da.

Natural source:   Common Name: Chikungunya virus strain S27-African prototype   Taxonomy ID: 371094   Superkingdom: Viruses   Kingdom: not available   Genus/species: Alphavirus Chikungunya virus

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

Entity Sequences (FASTA):
CHIKV_macro_domain: MKHHHHHHAPSYRVKRMDIA KNDEECVVNAANPRGLPGDG VCKAVYKKWPESFKNSATPV GTAKTVMCGTYPVIHAVGPN FSNYSESEGDRELAAAYREV AKEVTRLGVNSVAIPLLSTG VYSGGKDRLTQSLNHLFTAM DSTDADVVIYCRDKEWEKKI SEAIQMRT

Data sets:
Data typeCount
13C chemical shifts604
15N chemical shifts137
1H chemical shifts929

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CHIKV macro domain1

Entities:

Entity 1, CHIKV macro domain 168 residues - 18605.07 Da.

1   METLYSHISHISHISHISHISHISALAPRO
2   SERTYRARGVALLYSARGMETASPILEALA
3   LYSASNASPGLUGLUCYSVALVALASNALA
4   ALAASNPROARGGLYLEUPROGLYASPGLY
5   VALCYSLYSALAVALTYRLYSLYSTRPPRO
6   GLUSERPHELYSASNSERALATHRPROVAL
7   GLYTHRALALYSTHRVALMETCYSGLYTHR
8   TYRPROVALILEHISALAVALGLYPROASN
9   PHESERASNTYRSERGLUSERGLUGLYASP
10   ARGGLULEUALAALAALATYRARGGLUVAL
11   ALALYSGLUVALTHRARGLEUGLYVALASN
12   SERVALALAILEPROLEULEUSERTHRGLY
13   VALTYRSERGLYGLYLYSASPARGLEUTHR
14   GLNSERLEUASNHISLEUPHETHRALAMET
15   ASPSERTHRASPALAASPVALVALILETYR
16   CYSARGASPLYSGLUTRPGLULYSLYSILE
17   SERGLUALAILEGLNMETARGTHR

Samples:

sample_1: CHIKV macro domain, [U-99% 15N], 0.6 mM; soduim chloride 20 mM; Hepes 10 mM

sample_2: CHIKV macro domain, [U-99% 13C; U-99% 15N], 0.6 mM; soduim chloride 20 mM; Hepes 10 mM

sample_3: CHIKV macro domain 0.3 mM; soduim chloride 20 mM; Hepes 10 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 HN(CO)CAsample_2isotropicsample_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 HN(CA)COsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker Avance HD-III H 700 MHz

Related Database Links:

UNP Q8JUX6