BMRB Entry 15618

Name: NMR ASSIGNMENT OF THE DOMAIN 527-651 OF THE SARS-COV NONSTRUCTURAL PROTEIN NSP3
Published: 2008-01-30

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PDB ID: 2jzd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15618
MolProbity Validation Chart

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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:

NMR ASSIGNMENT OF THE DOMAIN 527-651 OF THE SARS-COV NONSTRUCTURAL PROTEIN NSP3

Deposition date:

2008-01-04

Original release date:

2008-01-30

Authors:

Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Joseph, Jeremiah; Saikatendu, Kumar; Neuman, Benjamin; Stevens, Raymond; Wilson, Ian; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt

Citation:

Citation: Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Joseph, Jeremiah; Neuman, Benjamin; Saikatendu, Kumar; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt. "Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold" J. Virol. 83, 1823-1836 (2009).
PubMed: 19052085

Assembly members:

Assembly members:
nsp3(527-651), polymer, 129 residues, Formula weight is not available

Natural source:

Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: not available Kingdom: Viruses Genus/species: not available Coronavirus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nsp3(527-651): GSHMGTVSWNLREMLAHAEE TRKLMPICMDVRAIMATIQR KYKGIKIQEGIVDYGVRFFF YTSKEPVASIITKLNSLNEP LVTMPIGYVTHGFNLEEAAR CMRSLKAPAVVSVSSPDAVT TYNGYLTSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	481
15N chemical shifts	130
1H chemical shifts	925

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nsp3(527-651)	1

Entities:

Entity 1, nsp3(527-651) 129 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLY

THR

VAL

SER

TRP

ASN

2

LEU

ARG

GLU

MET

LEU

ALA

HIS

ALA

GLU

3

THR

ARG

LYS

LEU

MET

PRO

ILE

CYS

MET

ASP

4

VAL

ARG

ALA

ILE

MET

ALA

THR

ILE

GLN

ARG

5

LYS

TYR

LYS

GLY

ILE

LYS

ILE

GLN

GLU

GLY

6

ILE

VAL

ASP

TYR

GLY

VAL

ARG

PHE

7

TYR

THR

SER

LYS

GLU

PRO

VAL

ALA

SER

ILE

8

ILE

THR

LYS

LEU

ASN

SER

LEU

ASN

GLU

PRO

9

LEU

VAL

THR

MET

PRO

ILE

GLY

TYR

VAL

THR

10

HIS

GLY

PHE

ASN

LEU

GLU

ALA

ARG

11

CYS

MET

ARG

SER

LEU

LYS

ALA

PRO

ALA

VAL

12

VAL

SER

VAL

SER

PRO

ASP

ALA

VAL

THR

13

THR

TYR

ASN

GLY

TYR

LEU

THR

SER

Samples:

sample_13C15N: nsp3(527-651), [U-99% 13C; U-98% 15N], 1.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; D2O 10%

sample_conditions_1: ionic strength: 0.227 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_13C15N	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_13C15N	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_13C15N	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_13C15N	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic region	sample_13C15N	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic region	sample_13C15N	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_13C15N	isotropic	sample_conditions_1
4D APSY-HNCOCA	sample_13C15N	isotropic	sample_conditions_1
4D APSY-HACANH	sample_13C15N	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_13C15N	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_13C15N	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

CARA v1.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - Creating Chemical Shift List, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker DRX 700 MHz

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