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BMRB Entry 30957

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30957
MolProbity Validation Chart

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Title: EmrE S64V Mutant Bound to tetra(4-fluorophenyl)phosphonium at pH 8.0   PubMed: 35181664

Deposition date: 2021-10-04 Original release date: 2022-02-18

Authors: Shcherbakov, A.; Spreacker, P.; Dregni, A.; Henzler-Wildman, K.; Hong, M.

Citation: Shcherbakov, A.; Spreacker, P.; Dregni, A.; Henzler-Wildman, K.; Hong, M.. "High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport"  Nat. Comm. 13, 991-991 (2022).

Assembly members:
entity_1, polymer, 110 residues, 11975.331 Da.
entity_VCJ, non-polymer, 411.351 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET15b

Entity Sequences (FASTA):
entity_1: MNPYIYLGGAILAEVIGTTL MKFSEGFTRLWPSVGTIICY CASFWLLAQTLAYIPTGIAY AIWVGVGIVLISLLSWGFFG QRLDLPAIIGMMLICAGVLI INLLSRSTPH

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts143
1H chemical shifts143

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_32

Entities:

Entity 1, unit_1 110 residues - 11975.331 Da.

1   METASNPROTYRILETYRLEUGLYGLYALA
2   ILELEUALAGLUVALILEGLYTHRTHRLEU
3   METLYSPHESERGLUGLYPHETHRARGLEU
4   TRPPROSERVALGLYTHRILEILECYSTYR
5   CYSALASERPHETRPLEULEUALAGLNTHR
6   LEUALATYRILEPROTHRGLYILEALATYR
7   ALAILETRPVALGLYVALGLYILEVALLEU
8   ILESERLEULEUSERTRPGLYPHEPHEGLY
9   GLNARGLEUASPLEUPROALAILEILEGLY
10   METMETLEUILECYSALAGLYVALLEUILE
11   ILEASNLEULEUSERARGSERTHRPROHIS

Entity 2, unit_3 - C24 H16 F4 P 1 - 411.351 Da.

1   VCJ

Samples:

sample_1: Multidrug Resistance Protein E (EmrE), [U-13C; U-15N; U-2H], 0.27 mg/uL; F4TPP 9.5 ug/uL; d54-DMPC, [U-99% 2H], 0.44 mg/uL

sample_conditions_1: ionic strength: 0.07 M; pH: 8.0; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D solid-state hNHsample_1isotropicsample_conditions_1
3D solid-state hCANHsample_1isotropicsample_conditions_1
3D solid-state hCONHsample_1isotropicsample_conditions_1
3D solid-state hCA(CO)NHsample_1isotropicsample_conditions_1
3D solid-state hCO(CA)NHsample_1isotropicsample_conditions_1
2D hNH-resolved 1H-19F REDORsample_1isotropicsample_conditions_1
3D solid-state H(NCACO)NHsample_1isotropicsample_conditions_1
3D solid-state hN(CACO)NHsample_1isotropicsample_conditions_1
3D solid-state h(CA)CB(CACO)NHsample_1isotropicsample_conditions_1
3D solid-state h(CA)CB(CA)NHsample_1isotropicsample_conditions_1
2D FF Exchangesample_1isotropicsample_conditions_1
2D water-edited solid-state hNHsample_1isotropicsample_conditions_1

Software:

HADDOCK vWebserver 2.4, Alexandre Bonvin and members of the computational structural biology group, Utrecht University - structure calculation

GROMACS v2019.1, UNIVERSITY OF GRONINGEN ROYAL INSTITUTE OF TECHNOLOGY UPPSALA UNIVERSITY - refinement

TopSpin v2.1-4.0, Bruker Biospin - collection, processing

NMRFAM-SPARKY v1.414, 1.470, NMRFAM - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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