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 16612

Title: Solid-state NMR structure of the M2 transmembrane peptide of the influenza A virus in DMPC lipid bilayers bound to deuterated amantadine   PubMed: 20130653

Authors: Cady, Sarah; Schmidt-Rohr, Klaus; Wang, Jun; Soto, Cinque; DeGrado, William; Hong, Mei

Citation: Cady, Sarah; Schmidt-Rohr, Klaus; Wang, Jun; Soto, Cinque; Degrado, William; Hong, Mei. "Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers."  Nature 463, 689-692 (2010).

Assembly members:
M2-TM, polymer, 25 residues, Formula weight is not available
308, non-polymer, 151.249 Da.

Natural source:   Common Name: Influenzavirus A   Taxonomy ID: 197911   Superkingdom: Virus   Kingdom: not available   Genus/species: Influenzavirus A not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
M2-TM: SSDPLVVAASIIGILHLILW ILDRL

Data sets:
Data typeCount
13C chemical shifts29
15N chemical shifts7

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1M2-TM_tetramer_monomer11
2M2-TM_tetramer_monomer21
3M2-TM_tetramer_monomer31
4M2-TM_tetramer_monomer41
5Amantadine2

Entities:

Entity 1, M2-TM_tetramer_monomer1 25 residues - Formula weight is not available

1   SERSERASPPROLEUVALVALALAALASER
2   ILEILEGLYILELEUHISLEUILELEUTRP
3   ILELEUASPARGLEU

Entity 2, Amantadine - C10 H17 N - 151.249 Da.

1   308

Samples:

SID-M2-TM_4x: M2-TM, [U-99% 13C; U-99% 15N] at S31, I32 and D44, 5.8 ± .1 mg; DMPC 21.6 ± .1 mg; NaH2PO4 10 mM; Na2HPO4 10 mM; EDTA 1 mM; NaN3 .1 mM; d15-1-aminoadamantane*HCl, [U-2H], .42 ± .05 mg

SID-M2-TM_1x: M2-TM, [U-99% 13C; U-99% 15N] at S31, I32 and D44, 5.0 ± .1 mg; DMPC 10.4 ± .1 mg; NaH2PO4 10 mM; Na2HPO4 10 mM; EDTA 1 mM; NaN3 0.1 mM; d15-1-aminoadamantane*HCl, [U-2H], 0.09 ± .05 mg

LVAG-M2-TM_4x: M2-TM, [U-99% 13C; U-99% 15N] at L26, V27, A29 and G34, 5.2 ± .1 mg; DMPC 19.9 ± .1 mg; NaH2PO4 10 mM; Na2HPO4 10 mM; EDTA 1 mM; NaN3 .1 mM; d15-1-aminoadamantane*HCl, [U-2H], 0.38 ± .05 mg

Unlabeled-M2-TM_4x: M2-TM, [U-99% 13C; U-99% 15N] at L26, V27, A29 and G34, 7 ± .1 mg; DMPC 27 ± .1 mg; NaH2PO4 10 mM; Na2HPO4 10 mM; EDTA 1 mM; NaN3 .1 mM; d15-1-aminoadamantane*HCl, [U-2H], 2.0 ± .05 mg

Unlabeled-M2-TM_1x: M2-TM, [U-99% 13C; U-99% 15N] at L26, V27, A29 and G34, 7 ± .1 mg; DMPC 27 ± .1 mg; NaH2PO4 10 mM; Na2HPO4 10 mM; EDTA 1 mM; NaN3 .1 mM; d15-1-aminoadamantane*HCl, [U-2H], 0.5 ± .05 mg

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 243 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C Spin DiffusionSID-M2-TM_4xsolidsample_conditions_1
2D 13C-13C Spin DiffusionSID-M2-TM_1xsolidsample_conditions_1
2D 13C-13C Spin DiffusionLVAG-M2-TM_4xsolidsample_conditions_1
2D 13C-15N HETCORSID-M2-TM_4xsolidsample_conditions_1
2D 13C-15N HETCORSID-M2-TM_1xsolidsample_conditions_1
2D 13C-15N HETCORLVAG-M2-TM_4xsolidsample_conditions_1
1D 2H-13C REDOR, single 13C pulseSID-M2-TM_4xsolidsample_conditions_1
1D 2H-13C REDOR, single 13C pulseSID-M2-TM_1xsolidsample_conditions_1
1D 2H-13C REDOR, single 13C pulseLVAG-M2-TM_4xsolidsample_conditions_1
1D 2H-13C REDOR, single 13C pulseSID-M2-TM_4xsolidsample_conditions_1
1D 2H-13C REDOR, single 2H pulseSID-M2-TM_4xsolidsample_conditions_1
1D 2H-13C REDOR, single 2H pulseSID-M2-TM_1xsolidsample_conditions_1
1D 2H-13C REDOR, single 2H pulseLVAG-M2-TM_4xsolidsample_conditions_1
2H Static Quadrupolar EchoUnlabeled-M2-TM_4xsolidsample_conditions_1
2H Static Quadrupolar EchoUnlabeled-M2-TM_1xsolidsample_conditions_1
2H Static Quadrupolar EchoLVAG-M2-TM_4xsolidsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - chemical shift assignment, collection, data analysis, peak picking, processing

MATLAB, The MathWorks - REDOR simulation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

xwinnmr, Bruker Biospin - chemical shift assignment, collection

NMR spectrometers:

  • Bruker Avance 400 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25234
PDB
DBJ BAB39517 BAB39519 BAD02354 BAD02364 BAD89308
EMBL CAA30887 CAA30889 CAA30891 CAA30893 CAA41929
GB AAA19192 AAA19194 AAA19196 AAA43091 AAA43276
PIR JN0393 MMIV2 S04057 S04061 S14617
REF NP_859035 YP_308670 YP_308840
SP A4GBX8 A4GCH6 A4GCJ8 A4GCK9 A4U7A7