BMRB Entry 15117

Name: Backbone H, C, N Chemical Shifts for Influenza A NS1 (1-73) Protein Bound to dsRNA
Published: 2008-02-11

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15117

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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:

Backbone H, C, N Chemical Shifts for Influenza A NS1 (1-73) Protein Bound to dsRNA

Deposition date:

2007-01-29

Original release date:

2008-02-11

Authors:

Yin, Cuifeng; Montelione, Gaetano

Citation:

Citation: Yin, Cuifeng; Khan, Javed; Swapna, Gurla; Ertekin, Asli; Krug, Robert; Tong, Liang; Montelione, Gaetano. "Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses." J. Biol. Chem. 282, 20584-20592 (2007).
PubMed: 17475623

Assembly members:

Assembly members:
NS1A, polymer, 73 residues, 8297.416 Da.
stranded_RNA_1, polymer, 16 residues, Formula weight is not available
stranded_RNA_2, polymer, 16 residues, Formula weight is not available

Natural source:

Natural source: Common Name: influenza A virus A/Udorn/72 Taxonomy ID: 11320 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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS1A: MDSNTVSSFQVDCFLWHVRK QVVDQELGDAPFLDRLRRDQ KSLRGRGSTLGLNIEAATHV GKQIVEKILKEES
stranded_RNA_1: CCAUCCUCUACAGGCG
stranded_RNA_2: CCAUCCUCUACAGGCG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	235
15N chemical shifts	87
1H chemical shifts	88

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS1A_chain 1	1
2	NS1A_chain 2	1
3	dsRNA	2
4	dsRNA	3

Entities:

Entity 1, NS1A_chain 1 73 residues - 8297.416 Da.

1

MET

ASP

SER

ASN

THR

VAL

SER

PHE

GLN

2

VAL

ASP

CYS

PHE

LEU

TRP

HIS

VAL

ARG

LYS

3

GLN

VAL

ASP

GLN

GLU

LEU

GLY

ASP

ALA

4

PRO

PHE

LEU

ASP

ARG

LEU

ARG

ASP

GLN

5

LYS

SER

LEU

ARG

GLY

ARG

GLY

SER

THR

LEU

6

GLY

LEU

ASN

ILE

GLU

ALA

THR

HIS

VAL

7

GLY

LYS

GLN

ILE

VAL

GLU

LYS

ILE

LEU

LYS

8

GLU

SER

Entity 2, dsRNA 16 residues - Formula weight is not available

1

C

A

U

C

U

C

U

A

2

C

A

G

C

G

Entity 3, dsRNA 16 residues - Formula weight is not available

1

C

A

U

C

U

C

U

A

2

C

A

G

C

G

Samples:

NS1A_(1-73): NS1A, [U-100% 13C; U-100% 15N], 0.1 mM; ammonium acetate 50 mM; ds-RNA 0.2 mM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NS1A_(1-73)	isotropic	sample_conditions_1
3D HNCO	NS1A_(1-73)	isotropic	sample_conditions_1
3D HNCA	NS1A_(1-73)	isotropic	sample_conditions_1
3D HNCACB	NS1A_(1-73)	isotropic	sample_conditions_1
3D HN(CO)CACB	NS1A_(1-73)	isotropic	sample_conditions_1

Software:

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

AutoAssign, Zimmerman, Moseley, Kulikowski, Montelione - data analysis

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Varian INOVA 600 MHz

BMRB	4317
PDB	1AIL 1NS1
DBJ	BAA01428
EMBL	CAA24288 CAC09426
GB	AAA43086 AAA43515 AAA43688 AAC36136 AAC36138
PRF	2005320B 2005320D
SP	P03494 P03495 P69277 P69278 Q1PUD3
AlphaFold	P03494 P03495 P69277 P69278 Q1PUD3