BMRB Entry 25368

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25368

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Title:
Backbone 1H, 13C and 15N chemical shifts for Staphylococcus aureus EF-GC3, a truncated form of elongation factor G comprising domains III-V.
Deposition date:
2014-11-26
Original release date:
2019-07-11
Authors:
Tomlinson, Jennifer; O'Neill, Alex; Homans, Steve; Zhuravleva, Anastasia; Kalverda, Arnout; Thompson, Gary
Citation:

Citation: Tomlinson, Jennifer; Thompson, Gary; Kalverda, Arnout; Zhuravleva, Anastasia; O'Neill, Alex. "A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance"  Sci. Rep. 6, 19524-19524 (2016).
PubMed: 26781961

Assembly members:

Assembly members:
EF-GC3, polymer, 301 residues, 33424.6284 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EF-GC3: MEFPEPVIHLSVEPKSKADQ DKMTQALVKLQEEDPTFHAH TDEETGQVIIGGMGELHLDI LVDRMKKEFNVECNVGAPMV SYRETFKSSAQVQGKFSRQS GGRGQYGDVHIEFTPNETGA GFEFENAIVGGVVPREYIPS VEAGLKDAMENGVLAGYPLI DVKAKLYDGSYHDVDSSEMA FKIAASLALKEAAKKCDPVI LEPMMKVTIEMPEEYMGDIM GDVTSRRGRVDGMEPRGNAQ VVNAYVPLSEMFGYATSLRS NTQGRGTYTMYFDHYAEVPK SIAEDIIKKNKGELEHHHHH H

Data sets:
Data typeCount
13C chemical shifts727
15N chemical shifts234
1H chemical shifts234

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1EF-GC31

Entities:

Entity 1, EF-GC3 301 residues - 33424.6284 Da.

This truncated protein begins at residue 401 of the full length EF-G protein and comprises domains III-V of EF-G. Residues 694-701 represent a non-native affinity tag

1   METGLUPHEPROGLUPROVALILEHISLEU
2   SERVALGLUPROLYSSERLYSALAASPGLN
3   ASPLYSMETTHRGLNALALEUVALLYSLEU
4   GLNGLUGLUASPPROTHRPHEHISALAHIS
5   THRASPGLUGLUTHRGLYGLNVALILEILE
6   GLYGLYMETGLYGLULEUHISLEUASPILE
7   LEUVALASPARGMETLYSLYSGLUPHEASN
8   VALGLUCYSASNVALGLYALAPROMETVAL
9   SERTYRARGGLUTHRPHELYSSERSERALA
10   GLNVALGLNGLYLYSPHESERARGGLNSER
11   GLYGLYARGGLYGLNTYRGLYASPVALHIS
12   ILEGLUPHETHRPROASNGLUTHRGLYALA
13   GLYPHEGLUPHEGLUASNALAILEVALGLY
14   GLYVALVALPROARGGLUTYRILEPROSER
15   VALGLUALAGLYLEULYSASPALAMETGLU
16   ASNGLYVALLEUALAGLYTYRPROLEUILE
17   ASPVALLYSALALYSLEUTYRASPGLYSER
18   TYRHISASPVALASPSERSERGLUMETALA
19   PHELYSILEALAALASERLEUALALEULYS
20   GLUALAALALYSLYSCYSASPPROVALILE
21   LEUGLUPROMETMETLYSVALTHRILEGLU
22   METPROGLUGLUTYRMETGLYASPILEMET
23   GLYASPVALTHRSERARGARGGLYARGVAL
24   ASPGLYMETGLUPROARGGLYASNALAGLN
25   VALVALASNALATYRVALPROLEUSERGLU
26   METPHEGLYTYRALATHRSERLEUARGSER
27   ASNTHRGLNGLYARGGLYTHRTYRTHRMET
28   TYRPHEASPHISTYRALAGLUVALPROLYS
29   SERILEALAGLUASPILEILELYSLYSASN
30   LYSGLYGLULEUGLUHISHISHISHISHIS
31   HIS

Samples:

sample_1: EF-GC3, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 mM; TrisHCl 20 mM; NaCl 300 mM; DTT 1 mM

standard_buffer: ionic strength: 0.310 M; pH: 8.000; pressure: 1.000 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)CAsample_1isotropicstandard_buffer
3D HNCOsample_1isotropicstandard_buffer
2D 1H-15N HSQC/HMQCsample_1isotropicstandard_buffer
HNCACO (H[N[ca[CO]]])sample_1isotropicstandard_buffer
3D HNCAsample_1isotropicstandard_buffer
3D HNCACBsample_1isotropicstandard_buffer
HNCOCACB (H[N[co[{CA|ca[C]}]]])sample_1isotropicstandard_buffer

Software:

CcpNmr_Analysis v2.1 - assignment

NMR spectrometers:

  • Varian Inova 600 MHz

Related Database Links:

NCBI P68790

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