BMRB Entry 16837

Name: HAV 3C C24S
Published: 2011-12-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16837

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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:

HAV 3C C24S

Deposition date:

2010-04-06

Original release date:

2011-12-15

Authors:

Blaum, Baerbel; Winfried, Wuensche; Andrew, Benie

Citation:

Citation: Blaum, Barbel; Wunsche, Winfried; Benie, Andrew; Kusov, Yuri; Peters, Hannelore; Gauss-Muller, Verena; Peters, Thomas; Sczakiel, Georg. "Functional binding of hexanucleotides to 3C protease of hepatitis A virus." Nucleic Acids Res. 40, 3042-3055 (2012).
PubMed: 22156376

Assembly members:

Assembly members:
HAV_3C_protease_C24S, polymer, 217 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Hepatitis A virus Taxonomy ID: 12092 Superkingdom: Virus Kingdom: not available Genus/species: Hepatovirus not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: ptac5SOD

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HAV_3C_protease_C24S: STLEIAGLVRKNLVQFGVGE KNGSVRWVMNALGVKDDWLL VPSHAYKFEKDYEMMEFYFN RGGTYYSISAGNVVIQSLDV GFQDVVLMKVPTIPKFRDIT QHFIKKGDVPRALNRLATLV TTVNGTPMLISEGPLKMEEK ATYVHKKNDGTTVDLTVDQA WRGKGEGLPGMCGGALVSSN QSIQNAILGIHVAGGNSILV AKLVTQEMFQNIDKKIE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	494
15N chemical shifts	157
1H chemical shifts	157

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HAV 3C C24S	1

Entities:

Entity 1, HAV 3C C24S 217 residues - Formula weight is not available

1

SER

THR

LEU

GLU

ILE

ALA

GLY

LEU

VAL

ARG

2

LYS

ASN

LEU

VAL

GLN

PHE

GLY

VAL

GLY

GLU

3

LYS

ASN

GLY

SER

VAL

ARG

TRP

VAL

MET

ASN

4

ALA

LEU

GLY

VAL

LYS

ASP

TRP

LEU

5

VAL

PRO

SER

HIS

ALA

TYR

LYS

PHE

GLU

LYS

6

ASP

TYR

GLU

MET

GLU

PHE

TYR

PHE

ASN

7

ARG

GLY

THR

TYR

SER

ILE

SER

ALA

8

GLY

ASN

VAL

ILE

GLN

SER

LEU

ASP

VAL

9

GLY

PHE

GLN

ASP

VAL

LEU

MET

LYS

VAL

10

PRO

THR

ILE

PRO

LYS

PHE

ARG

ASP

ILE

THR

11

GLN

HIS

PHE

ILE

LYS

GLY

ASP

VAL

PRO

12

ARG

ALA

LEU

ASN

ARG

LEU

ALA

THR

LEU

VAL

13

THR

VAL

ASN

GLY

THR

PRO

MET

LEU

ILE

14

SER

GLU

GLY

PRO

LEU

LYS

MET

GLU

LYS

15

ALA

THR

TYR

VAL

HIS

LYS

ASN

ASP

GLY

16

THR

VAL

ASP

LEU

THR

VAL

ASP

GLN

ALA

17

TRP

ARG

GLY

LYS

GLY

GLU

GLY

LEU

PRO

GLY

18

MET

CYS

GLY

ALA

LEU

VAL

SER

ASN

19

GLN

SER

ILE

GLN

ASN

ALA

ILE

LEU

GLY

ILE

20

HIS

VAL

ALA

GLY

ASN

SER

ILE

LEU

VAL

21

ALA

LYS

LEU

VAL

THR

GLN

GLU

MET

PHE

GLN

22

ASN

ILE

ASP

LYS

ILE

GLU

Samples:

sample_1: HAV 3C protease C24S, [U-100% 13C; U-100% 15N; U-75% 2H], 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 200 mM; pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

PDB	1HAV 1QA7 2A4O 2CXV 2H6M 2H9H 2HAL
DBJ	BAA35102 BAA35103 BAA35104 BAA35105 BAA35106
EMBL	CAA33491 CAA50195 CAA53024 CAA53025 CAA53026
GB	AAA45465 AAA45466 AAA45467 AAA45468 AAA45469
PIR	GNNYHB
REF	NP_041007 NP_041008 NP_740558
SP	A3FMB2 A5LGW7 P06441 P08617 P13901
AlphaFold	A3FMB2 A5LGW7 P06441 P08617 P13901