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 50411

Title: EmrE S64V Mutant Bound to tetra(4-fluorophenyl)phosphonium at pH 5.8

Deposition date: 2020-07-27 Original release date: 2020-11-30

Authors: Shcherbakov, Alexander; Hong, Mei

Citation: Shcherbakov, Alexander; Hisao, Grant; Mandala, Venkata; Thomas, Nathan; Soltani, Mohammad; Salter, E.; Davis, James; Henzler-Wildman, Katherine; Hong, Mei. "Structure and Dynamics of the Drug-Bound Bacterial Transporter EmrE in Lipid Bilayers"  Nat. Commun. ., .-..

Assembly members:
entity_1, polymer, 110 residues, Formula weight is not available
tetrakis(4-fluorophenyl)phosphanium, 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   Vector: pET15b

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

Data sets:
Data typeCount
13C chemical shifts459
15N chemical shifts135
1H chemical shifts133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EmrE S64V Mutant, A monomer1
2EmrE S64V Mutant, B monomer1
3F4TPP2

Entities:

Entity 1, EmrE S64V Mutant, A monomer 110 residues - Formula weight is not available

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

Entity 2, F4TPP - C24 H16 F4 P - 411.351 Da.

1   VCJ

Samples:

sample_1: EmrE-S64V, [U-99% 13C; U-99% 15N], 0.26 mg/uL; F4TPP 9.5 ug/uL; DMPC 0.41 mg/uL; MES 50 mM; sodium chloride 20 mM

sample_2: EmrE-S64V, [U-13C; U-15N; U-2H], 0.27 mg/uL; F4TPP 9.5 ug/uL; d54-DMPC, [U-99% 2H], 0.44 mg/uL; MES 50 mM; sodium chloride 20 mM

sample_3: EmrE-S64V, [U-99% 15N], 0.13 mg/uL; F4TPP 5.4 ug/uL; DMPC 0.46 mg/uL; MES 50 mM; sodium chloride 20 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 5.8; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
3D solid-state hCANHsample_2isotropicsample_conditions_1
3D solid-state hCONHsample_2isotropicsample_conditions_1
3D solid-state hCA(CO)NHsample_2isotropicsample_conditions_1
3D solid-state hCO(CA)NHsample_2isotropicsample_conditions_1
2D CC CORDsample_3isotropicsample_conditions_1
3D NCACXsample_3isotropicsample_conditions_1
1D 19Fsample_1isotropicsample_conditions_1
2D FF Exchangesample_1isotropicsample_conditions_1
19F-13C Double-Quantum Cross Polarizationsample_1isotropicsample_conditions_1
2D solid-state hNHsample_2isotropicsample_conditions_1
1D 13C-19F REDORsample_1isotropicsample_conditions_1
2D hNH-resolved 1H-19F REDORsample_2isotropicsample_conditions_1

Software:

HADDOCK vWebserver 2.4 - structure solution

TOPSPIN v2.1-4.0 - processing

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

GROMACS v2019.1 - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE NEO 700 MHz
  • Bruker Avance II 800 MHz

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