BMRB Entry 15222

Name: PV-3C
Published: 2007-05-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15222

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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:

PV-3C

Deposition date:

2007-04-25

Original release date:

2007-05-18

Authors:

Amero, Carlos; Arnold, Jamie; Cameron, Craig; Foster, Mark

Citation:

Citation: Amero, Carlos; Arnold, Jamie; Moustafa, I.; Cameron, Craig; Foster, Mark. "Identification of the oriI-binding site of poliovirus 3C protein by nuclear magnetic resonance spectroscopy" J. Virol. 82, 4363-4370 (2008).
PubMed: 18305026

Assembly members:

Assembly members:
3C, polymer, 193 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: 138953 Superkingdom: Viruses Kingdom: not available Genus/species: Enterovirus Poliovirus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET26Ub-PV 3C C147A C153S CHIS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
3C: GPGFDYAVAMAKRNIVTATT SKGEFTMLGVHDNVAILPTH ASPGESIVIDGKEVEILDAK ALEDQAGTNLEITIITLKRN EKFRDIRPHIPTQITETNDG VLIVNTSKYPNMYVPVGAVT EQGYLNLGGRQTARTLMYNF PTRAGQAGGVITSTGKVIGM HVGGNGSHGFAAALKRSYFT QSQGSSGHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	146
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PV-3C	1

Entities:

Entity 1, PV-3C 193 residues - Formula weight is not available

1

GLY

PRO

GLY

PHE

ASP

TYR

ALA

VAL

ALA

MET

2

ALA

LYS

ARG

ASN

ILE

VAL

THR

ALA

THR

3

SER

LYS

GLY

GLU

PHE

THR

MET

LEU

GLY

VAL

4

HIS

ASP

ASN

VAL

ALA

ILE

LEU

PRO

THR

HIS

5

ALA

SER

PRO

GLY

GLU

SER

ILE

VAL

ILE

ASP

6

GLY

LYS

GLU

VAL

GLU

ILE

LEU

ASP

ALA

LYS

7

ALA

LEU

GLU

ASP

GLN

ALA

GLY

THR

ASN

LEU

8

GLU

ILE

THR

ILE

THR

LEU

LYS

ARG

ASN

9

GLU

LYS

PHE

ARG

ASP

ILE

ARG

PRO

HIS

ILE

10

PRO

THR

GLN

ILE

THR

GLU

THR

ASN

ASP

GLY

11

VAL

LEU

ILE

VAL

ASN

THR

SER

LYS

TYR

PRO

12

ASN

MET

TYR

VAL

PRO

VAL

GLY

ALA

VAL

THR

13

GLU

GLN

GLY

TYR

LEU

ASN

LEU

GLY

ARG

14

GLN

THR

ALA

ARG

THR

LEU

MET

TYR

ASN

PHE

15

PRO

THR

ARG

ALA

GLY

GLN

ALA

GLY

VAL

16

ILE

THR

SER

THR

GLY

LYS

VAL

ILE

GLY

MET

17

HIS

VAL

GLY

ASN

GLY

SER

HIS

GLY

PHE

18

ALA

LEU

LYS

ARG

SER

TYR

PHE

THR

19

GLN

SER

GLN

GLY

SER

GLY

HIS

20

HIS

Samples:

sample_1: 3C, [U-100% 13C; U-100% 15N; 80% 2H], 0.5 mM; HEPES 10 mM; sodium chloride 100 mM; D2O 10%; TSP 1%

sample_2: 3C, [U-100% 15N], 0.5 mM; HEPES 10 mM; sodium chloride 100 mM; D2O 10%; TSP 1%

sample_conditions_1: pH: 8.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker DMX 600 MHz
Bruker DMX 800 MHz

PDB	1L1N 2IJD 4DCD
EMBL	CAA24461 CAA24465 CAA25246 CAA25247 CAA25444
GB	AAA46914 AAL75969 AAL75970 AAM09803 AAM09805
REF	NP_041277 NP_740476 YP_007353734
SP	P03300 P03301 P03302
AlphaFold	P03300 P03301 P03302