BMRB Entry 50593

Name: nsP3 VEEV
Published: 2021-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50593

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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:

nsP3 VEEV

Deposition date:

2020-11-23

Original release date:

2021-06-30

Authors:

Agback, Peter; Shernyukov, Andrey; Dominguez, Francisco; Agback, Tatiana; Frolova, Elena

Citation:

Citation: Agback, Peter; Shernyukov, Andrey; Dominguez, Francisco; Agback, Tatiana; Frolova, Elena. "Novel NMR Assignment Strategy Reveals Structural Heterogeneity in Solution of the nsP3 HVD Domain of Venezuelan Equine Encephalitis Virus." Molecules 25, 5824-5824 (2020).
PubMed: 33321815

Assembly members:

Assembly members:
entity_1, polymer, 189 residues, Formula weight is not available

Natural source:

Natural source: Common Name: alphavirus togaviridae Taxonomy ID: 11018 Superkingdom: Viruses Kingdom: not available Genus/species: alphavirus togaviridae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pE-SUMOpro-3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSLWVETPPVDETPEPSAEN QSTEGTPEQPPLITEDETRT RTPEPIIIEEEEEDSISLLS DGPTHQVLQVEADIHGPPSV SSSSWSIPHASDFDVDSLSI LDTLEGASVTSGATSAETNS YFAKSMEFLARPVPAPRTVF RNPPHPAPRTRTPSLAPSRA CSRTSLVSTPPGVNRVITRE ELEALTPSR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	517
15N chemical shifts	150
1H chemical shifts	332

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nsP3	1

Entities:

Entity 1, nsP3 189 residues - Formula weight is not available

1

GLY

SER

LEU

TRP

VAL

GLU

THR

PRO

VAL

2

ASP

GLU

THR

PRO

GLU

PRO

SER

ALA

GLU

ASN

3

GLN

SER

THR

GLU

GLY

THR

PRO

GLU

GLN

PRO

4

PRO

LEU

ILE

THR

GLU

ASP

GLU

THR

ARG

THR

5

ARG

THR

PRO

GLU

PRO

ILE

GLU

6

GLU

ASP

SER

ILE

SER

LEU

SER

7

ASP

GLY

PRO

THR

HIS

GLN

VAL

LEU

GLN

VAL

8

GLU

ALA

ASP

ILE

HIS

GLY

PRO

SER

VAL

9

SER

TRP

SER

ILE

PRO

HIS

ALA

10

SER

ASP

PHE

ASP

VAL

ASP

SER

LEU

SER

ILE

11

LEU

ASP

THR

LEU

GLU

GLY

ALA

SER

VAL

THR

12

SER

GLY

ALA

THR

SER

ALA

GLU

THR

ASN

SER

13

TYR

PHE

ALA

LYS

SER

MET

GLU

PHE

LEU

ALA

14

ARG

PRO

VAL

PRO

ALA

PRO

ARG

THR

VAL

PHE

15

ARG

ASN

PRO

HIS

PRO

ALA

PRO

ARG

THR

16

ARG

THR

PRO

SER

LEU

ALA

PRO

SER

ARG

ALA

17

CYS

SER

ARG

THR

SER

LEU

VAL

SER

THR

PRO

18

PRO

GLY

VAL

ASN

ARG

VAL

ILE

THR

ARG

GLU

19

GLU

LEU

GLU

ALA

LEU

THR

PRO

SER

ARG

Samples:

sample_1: nsP3, [U-100% 13C; U-100% 15N], 765 ± 15 uM; TCEP 2 mM; NaN3 1 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5 - collection

TOPSPIN v4.0.5 - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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