BMRB Entry 4317

Name: 1H, 13C, and 15N Chemical Shift Assignments for NS1(1-73)
Published: 2004-12-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4317

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 13C, and 15N Chemical Shift Assignments for NS1(1-73)

Deposition date:

1999-03-12

Original release date:

2004-12-07

Authors:

Chien, Chen-ya; Montelione, Gaetano

Citation:

Citation: Chien, Chen-ya; Tejero, R.; Huang, Y.; Zimmerman, D.; Rios, C.; Krug, R.; Montelione, Gaetano. "A novel RNA-binding motif in influenza A virus non-structural protein 1" Nat. Struct. Biol. 4, 891-. (1997).

Assembly members:

Assembly members:
Non-structural protein 1, polymer, 73 residues, 8300 Da.

Natural source:

Natural source: Common Name: Flu Virus Taxonomy ID: 11320 Superkingdom: Viruses Kingdom: not available Genus/species: Influenza virus A and B group Influenza A Virus

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Non-structural protein 1: MDSNTVSSFQVDCFLWHVRK QVVDQELGDAPFLDRLRRDQ KSLRGRGSTLGLNIEAATHV GKQIVEKILKEES

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
13C chemical shifts	303
15N chemical shifts	85
1H chemical shifts	534

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS1(1-73) subunit 1	1
2	NS1(1-73) subunit 2	1

Entities:

Entity 1, NS1(1-73) subunit 1 73 residues - 8300 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

Samples:

sample_1: NS1(1-73) dimer 2.0 mM; NH4)Ac 50 mM; D2O 5%; H2O 95%

sample_2: NS1(1-73) dimer, [U-100% 15N], 2.5 mM; NH4)Ac 50 mM; D2O 5%; H2O 95%

sample_3: NS1(1-73) dimer, [U-100% 15N; U-100% 13C], 2.0 mM; NH4)Ac 50 mM; D2O 5%; H2O 95%

condition_1: pH: 6.0 na; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	not available	not available	condition_1
HNCO	not available	not available	condition_1
CANH	not available	not available	condition_1
CA(CO)NH	not available	not available	condition_1
H(CA)NH	not available	not available	condition_1
H(CA)(CO)NH	not available	not available	condition_1
CBCANH	not available	not available	condition_1
CBCA(CO)NH	not available	not available	condition_1
HCC(CO)NH-TOCSY	not available	not available	condition_1
HCCH-COSY	not available	not available	condition_1
4 channel probe with pulse field gradient	not available	not available	condition_1

Software:

vnmr v5.3 - Data processing

NMRcompass - Spectra analysis and peakpicking

AUTOASSIGN - 1H, 13C, 15N resonance assignment, Software developed in Montelione lab [Zimmerman et al. (1997) J. Mol. Biol. 269:592-610] for automating the peak assignment

NMR spectrometers:

Varian . 500 MHz
Varian . 600 MHz

BMRB	15117
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