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 25788

Title: Two-fold symmetric structure of the 18-60 construct of S31N M2 from Influenza A in lipid bilayers

Deposition date: 2015-09-01 Original release date: 2016-02-24

Authors: Andreas, Loren; Reese, Marcel; Eddy, Matthew; Gelev, Vladimir; Ni, Qing Zhe; Miller, Eric; Emsley, Lyndon; Pintacuda, Guido; Chou, James; Griffin, Robert

Citation: Andreas, Loren; Reese, Marcel; Eddy, Matthew; Gelev, Vladimir; Ni, Qing Zhe; Miller, Eric; Emsley, Lyndon; Pintacuda, Guido; Chou, James; Griffin, Robert. "Structure and Mechanism of the Influenza A M218-60 Dimer of Dimers"  J. Am. Chem. Soc. 137, 14877-14886 (2015).

Assembly members:
matrix_protein_2, polymer, 43 residues, Formula weight is not available

Natural source:   Common Name: Influenza A virus   Taxonomy ID: 385599   Superkingdom: Viruses   Kingdom: not available   Genus/species: Influenzavirus A Influenza A virus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET

Entity Sequences (FASTA):
matrix_protein_2: RSNDSSDPLVVAANIIGILH LILWILDRLFFKSIYRFFEH GLK

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts59
1H chemical shifts90

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21
3entity_31
4entity_41

Entities:

Entity 1, entity_1 43 residues - Formula weight is not available

1   ARGSERASNASPSERSERASPPROLEUVAL
2   VALALAALAASNILEILEGLYILELEUHIS
3   LEUILELEUTRPILELEUASPARGLEUPHE
4   PHELYSSERILETYRARGPHEPHEGLUHIS
5   GLYLEULYS

Samples:

U-13C-15N_S31N_M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine 50 % w/w; matrix protein 2, [U-13C,15N], 50 % w/w; H2O 100%

U-13C-15N-12C-14N-ILFY-M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine 50 % w/w; matrix protein 2, U-13C,15N-[12C,14N-ILFY], 50 % w/w; H2O 100%

1-13C-Glucose-M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine 50 % w/w; matrix protein 2, [1-13C]-Glucose, 50 % w/w; H2O 100%

1-6-13C2-Glucose-M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine 50 % w/w; matrix protein 2, [1,6-13C2]-Glucose, 50 % w/w; H2O 100%

U-13C-15N-2H-12C-13C2H21H_1-Ile_12C-13Ca-13C-13C2H21H_2-Leu_12C-13C2H21H_2-Val_M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine, aliphatic chain [U-2H], 50 % w/w; matrix protein 2, U-13C,15N,2H-[12C,13C2H21H 1-Ile, 12C,13Ca,13C',13C2H21H 2-Leu, 12C,13C2H21H 2-Val], 50 % w/w; H2O 100%

U-13C-15N-2H-13CH3_1-Ile_M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine, aliphatic chain [U-2H], 50 % w/w; matrix protein 2, U-13C,15N,2H-[13CH3 1-Ile], 50 % w/w; H2O 100%

U-13C-15N-2H-13C2H21H_2-Leu_13C2H21H_2-Val-M2: sodium phosphate 40 ± 1 mM; glutamic acid 30 ± 1 mM; sodium azide 3 ± 1 mM; 1,2-diphytanoyl-sn-glycero-3-phosphocholine, aliphatic chain [U-2H], 50 % w/w; matrix protein 2, U-13C,15N,2H-[13C2H21H 2-Leu, 13C2H21H 2-Val], 50 % w/w; H2O 100%

sample_conditions_1: pH: 7.8; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D ZF-TEDORU-13C-15N_S31N_M2anisotropicsample_conditions_1
3D ZF-TEDOR-RFDRU-13C-15N_S31N_M2anisotropicsample_conditions_1
2D HNU-13C-15N_S31N_M2anisotropicsample_conditions_1
3D (H) CaNHU-13C-15N-12C-14N-ILFY-M2anisotropicsample_conditions_1
2D PARU-13C-15N_S31N_M2anisotropicsample_conditions_1
2D PDSDU-13C-15N_S31N_M2anisotropicsample_conditions_1
2D ZF-TEDOR1-6-13C2-Glucose-M2anisotropicsample_conditions_1
2D RFDR1-6-13C2-Glucose-M2anisotropicsample_conditions_1
3D 1H-1H RFDRU-13C-15N-12C-14N-ILFY-M2anisotropicsample_conditions_1
4D HCHHCHU-13C-15N-12C-14N-ILFY-M2anisotropicsample_conditions_1
2D C-HU-13C-15N-2H-12C-13C2H21H_1-Ile_12C-13Ca-13C-13C2H21H_2-Leu_12C-13C2H21H_2-Val_M2anisotropicsample_conditions_1

Software:

TALOS+, Cornilescu, Delaglio and Bax - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 1000 MHz
  • FBML Cambridge Instruments 750 MHz

Related Database Links:

PDB

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