BMRB Entry 17451

Name: Central domain of RSV M2-1
Published: 2011-05-03

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PDB ID: 2l9j
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17451
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Central domain of RSV M2-1

Deposition date:

2011-02-09

Original release date:

2011-05-03

Authors:

Dubosclard, Virginie; Blondot, Marie-Lise; Eleouet, Jean-Francois; Bontems, Francois; Sizun, Christina

Citation:

Citation: Dubosclard, Virginie; Blondot, Marie-Lise; Eleouet, Jean-Francois; Bontems, Francois; Sizun, Christina. "1H, 13C, and 15N resonance assignment of the central domain of hRSV transcription antitermination factor M2-1." Biomol. NMR Assignments 5, 237-239 (2011).
PubMed: 21523439

Assembly members:

Assembly members:
M2-1, polymer, 121 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human syncytial respiratory virus Taxonomy ID: 11245 Superkingdom: virus Kingdom: not available Genus/species: Pneumovirus Human respiratory syncytial virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
M2-1: GSEISGAAELDRTEEYALGV VGVLESYIGSINNITKQSAC VAMSKLLTELNSDDIKKLRD NEEPNSPKIRVYNTVISYIE SNRKNNKQTIHLLKRLPADV LKKTIKNTLDIHKSITINNP K

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1
- RDC_list_2

Data type	Count
13C chemical shifts	533
15N chemical shifts	129
1H chemical shifts	889
residual dipolar couplings	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	M2-1	1

Entities:

Entity 1, M2-1 121 residues - Formula weight is not available

The two first residues GS are left after cleavage of the N-terminal GST tag. The M2-1 sequence starts at Glu59 and ends with Lys177.

1

GLY

SER

GLU

ILE

SER

GLY

ALA

GLU

LEU

2

ASP

ARG

THR

GLU

TYR

ALA

LEU

GLY

VAL

3

VAL

GLY

VAL

LEU

GLU

SER

TYR

ILE

GLY

SER

4

ILE

ASN

ILE

THR

LYS

GLN

SER

ALA

CYS

5

VAL

ALA

MET

SER

LYS

LEU

THR

GLU

LEU

6

ASN

SER

ASP

ILE

LYS

LEU

ARG

ASP

7

ASN

GLU

PRO

ASN

SER

PRO

LYS

ILE

ARG

8

VAL

TYR

ASN

THR

VAL

ILE

SER

TYR

ILE

GLU

9

SER

ASN

ARG

LYS

ASN

LYS

GLN

THR

ILE

10

HIS

LEU

LYS

ARG

LEU

PRO

ALA

ASP

VAL

11

LEU

LYS

THR

ILE

LYS

ASN

THR

LEU

ASP

12

ILE

HIS

LYS

SER

ILE

THR

ILE

ASN

PRO

13

LYS

Samples:

M21-15N13C: M2-1, [U-100% 13C; U-100% 15N], 0.13 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; H2O 93%; D2O 7%

M21-13C: M2-1, [U-100% 13C], 0.1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; D2O 100%

M21-15N-c12e5: M2-1, [U-100% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; c12e5 0.055 v/v; Hexanol 0.017 v/v; H2O 93%; D2O 7%

M21-15N-gel: M2-1, [U-100% 15N], 0.12 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; acrylamide/bisacryamide 6%; H2O 93%; D2O 7%

M21-15N: M2-1, [U-100% 15N], 0.12 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	M21-15N13C	isotropic	sample_conditions_1
3D HNCO	M21-15N13C	isotropic	sample_conditions_1
3D HNCA	M21-15N13C	isotropic	sample_conditions_1
3D HN(CO)CA	M21-15N13C	isotropic	sample_conditions_1
3D HNCACB	M21-15N13C	isotropic	sample_conditions_1
3D CBCA(CO)NH	M21-15N13C	isotropic	sample_conditions_1
3D 1H-15N NOESY	M21-15N	isotropic	sample_conditions_1
2D 1H-13C HSQC	M21-13C	isotropic	sample_conditions_1
3D HCCH-TOCSY	M21-13C	isotropic	sample_conditions_1
3D HCCH-TOCSY aromatic	M21-13C	isotropic	sample_conditions_1
3D CCH-TOCSY	M21-13C	isotropic	sample_conditions_1
3D 1H-13C NOESY	M21-13C	isotropic	sample_conditions_1
2D HBCBCGCDHD	M21-13C	isotropic	sample_conditions_1
2D 1H-15N IPAP HSQC	M21-15N-c12e5	anisotropic	sample_conditions_1
2D 1H-15N IPAP HSQC	M21-15N-gel	anisotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis, peak picking

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 950 MHz

PDB	2L9J 4C3B 4C3D 4C3E
DBJ	BAA00106
GB	AAB59860 AAB86665 AAB86677 AAC14903 AAC55971
REF	NP_044597
SP	P04545
AlphaFold	P04545