BMRB Entry 30370

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30370
MolProbity Validation Chart

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Title:
Solution NMR structure of uncharacterized protein YejG representing the first structure from PF13989
Deposition date:
2017-11-01
Original release date:
2018-10-31
Authors:
Mohanty, B.; Finn, T.; Macindoe, I.; Zhong, J.; Patrick, W.; Mackay, J.
Citation:

Citation: Mohanty, Biswaranjan; Hanson-Manful, Paulina; Finn, Thomas; Chambers, Cecilia; McKellar, James; Macindoe, Ingrid; Helder, Stephanie; Setiyaputra, Surya; Zhong, Yichen; Mackay, Joel; Patrick, Wayne. "The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G."  Proteins 87, 699-705 (2019).
PubMed: 30958578

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 12557.149 Da.

Natural source:

Natural source:   Common Name: Escherichia coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6p

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPTSLQLSIVHRLPQNYRWS AGFAGSKVEPIPQNGPCGDN SLVALKLLSPDGDNAWSVMY KLSQALSDIEVPCSVLECEG EPCLFVNRQDEFAATCRLKN FGVAIAEPFSNYNPF

Data sets:
Data typeCount
13C chemical shifts439
15N chemical shifts106
1H chemical shifts689

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 115 residues - 12557.149 Da.

1   GLYPROTHRSERLEUGLNLEUSERILEVAL
2   HISARGLEUPROGLNASNTYRARGTRPSER
3   ALAGLYPHEALAGLYSERLYSVALGLUPRO
4   ILEPROGLNASNGLYPROCYSGLYASPASN
5   SERLEUVALALALEULYSLEULEUSERPRO
6   ASPGLYASPASNALATRPSERVALMETTYR
7   LYSLEUSERGLNALALEUSERASPILEGLU
8   VALPROCYSSERVALLEUGLUCYSGLUGLY
9   GLUPROCYSLEUPHEVALASNARGGLNASP
10   GLUPHEALAALATHRCYSARGLEULYSASN
11   PHEGLYVALALAILEALAGLUPROPHESER
12   ASNTYRASNPROPHE

Samples:

sample_1: Bi-tris 20 mM; NaCl 50 mM; PMSF 0.2 mM; TCEP 1 mM; YejG, [U-13C; U-15N], 600 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D [15N,1H]-HSQCsample_1not availablesample_conditions_1
3D 15N-resolved [1H,1H]-NOESYsample_1not availablesample_conditions_1
3D 13Cali-resolved [1H,1H]-NOESYsample_1not availablesample_conditions_1
3D 13Caro-resolved [1H,1H]-NOESYsample_1not availablesample_conditions_1
2D [13Cali,1H]-HSQC (multiplicity edited)sample_1not availablesample_conditions_1
2D [13Caro,1H]-HSQCsample_1not availablesample_conditions_1
2D 1H-1H NOESYsample_1not availablesample_conditions_1
3D NUS HNCAsample_1not availablesample_conditions_1
3D NUS HNCACBsample_1not availablesample_conditions_1
3D NUS CBCA(CO)NHsample_1not availablesample_conditions_1
3D NUS HN(CA)COsample_1not availablesample_conditions_1
3D NUS HNCOsample_1not availablesample_conditions_1
3D NUS HBHA(CO)NHsample_1not availablesample_conditions_1
3D NUS HNHAsample_1not availablesample_conditions_1
3D NUS (H)CC(CO)NHsample_1not availablesample_conditions_1
15N{1H}-NOEsample_1not availablesample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp, Koradi, Billeter and Guntert - refinement

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance III 600 MHz
  • Bruker Avance III 800 MHz

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