BMRB Entry 25788

Name: Two-fold symmetric structure of the 18-60 construct of S31N M2 from Influenza A in lipid bilayers
Published: 2016-02-24

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PDB ID: 2n70
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25788
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
matrix_protein_2: RSNDSSDPLVVAANIIGILH LILWILDRLFFKSIYRFFEH GLK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	250
15N chemical shifts	59
1H chemical shifts	90

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1
3	entity_3	1
4	entity_4	1

Entities:

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

1

ARG

SER

ASN

ASP

SER

ASP

PRO

LEU

VAL

2

VAL

ALA

ASN

ILE

GLY

ILE

LEU

HIS

3

LEU

ILE

LEU

TRP

ILE

LEU

ASP

ARG

LEU

PHE

4

PHE

LYS

SER

ILE

TYR

ARG

PHE

GLU

HIS

5

GLY

LEU

LYS

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:

Name	Sample	Sample state	Sample conditions
2D ZF-TEDOR	U-13C-15N_S31N_M2	anisotropic	sample_conditions_1
3D ZF-TEDOR-RFDR	U-13C-15N_S31N_M2	anisotropic	sample_conditions_1
2D HN	U-13C-15N_S31N_M2	anisotropic	sample_conditions_1
3D (H) CaNH	U-13C-15N-12C-14N-ILFY-M2	anisotropic	sample_conditions_1
2D PAR	U-13C-15N_S31N_M2	anisotropic	sample_conditions_1
2D PDSD	U-13C-15N_S31N_M2	anisotropic	sample_conditions_1
2D ZF-TEDOR	1-6-13C2-Glucose-M2	anisotropic	sample_conditions_1
2D RFDR	1-6-13C2-Glucose-M2	anisotropic	sample_conditions_1
3D 1H-1H RFDR	U-13C-15N-12C-14N-ILFY-M2	anisotropic	sample_conditions_1
4D HCHHCH	U-13C-15N-12C-14N-ILFY-M2	anisotropic	sample_conditions_1
2D C-H	U-13C-15N-2H-12C-13C2H21H_1-Ile_12C-13Ca-13C-13C2H21H_2-Leu_12C-13C2H21H_2-Val_M2	anisotropic	sample_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