BMRB Entry 16008

Name: Solution structure of the SARS-unique domain-C from the nonstructural protein 3 (nsp3) of the severe acute respiratory syndrome coronavirus
Published: 2009-01-06

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16008

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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:

Solution structure of the SARS-unique domain-C from the nonstructural protein 3 (nsp3) of the severe acute respiratory syndrome coronavirus

Deposition date:

2008-10-28

Original release date:

2009-01-06

Authors:

Johnson, Margaret; Mohanty, Biswaranjan; Pedrini, Bill; Serrano, Pedro; Chatterjee, Amarnath; Herrmann, Torsten; Joseph, Jeremiah; Saikatendu, Kumar; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt

Citation:

Citation: Serrano, Pedro; Johnson, Margaret; Chatterjee, Amarnath; Neuman, Benjamin; Joseph, Jeremiah; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt. "Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3." J. Virol. 83, 12998-13008 (2009).
PubMed: 19828617

Assembly members:

Assembly members:
SUD-C, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: 227984 Superkingdom: virus Kingdom: not available Genus/species: Coronavirus SARS coronavirus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SUD-C: GSEEHFVETVSLAGSYRDWS YSGQRTELGVEFLKRGDKIV YHTLESPVEFHLDGEVLSLD KLKSLLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	291
15N chemical shifts	66
1H chemical shifts	466

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SUD-C	1

Entities:

Entity 1, SUD-C 67 residues - Formula weight is not available

1

GLY

SER

GLU

HIS

PHE

VAL

GLU

THR

VAL

2

SER

LEU

ALA

GLY

SER

TYR

ARG

ASP

TRP

SER

3

TYR

SER

GLY

GLN

ARG

THR

GLU

LEU

GLY

VAL

4

GLU

PHE

LEU

LYS

ARG

GLY

ASP

LYS

ILE

VAL

5

TYR

HIS

THR

LEU

GLU

SER

PRO

VAL

GLU

PHE

6

HIS

LEU

ASP

GLY

GLU

VAL

LEU

SER

LEU

ASP

7

LYS

LEU

LYS

SER

LEU

SER

Samples:

sample_1: SUD-C, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 20 mM; sodium phosphate 20 mM; sodium azide 2.8 mM

sample_conditions_1: ionic strength: 0.0628 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_1	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_1	isotropic	sample_conditions_1
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

MATCH, Volk, Herrmann and Wuthrich - chemical shift assignment

ASCAN, Fiorito, Herrmann, Damberger and Wuthrich - chemical shift assignment

CARA, Keller and Wuthrich - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	16613
PDB	2KAF 2KQV 2KQW
DBJ	BAC81346 BAC81347 BAC81360 BAC81361 BAC81374
GB	AAP13439 AAP13442 AAP13566 AAP13575 AAP30028
REF	NP_828849 NP_828850 NP_828862
SP	P0C6U8 P0C6X7
AlphaFold	P0C6U8 P0C6X7