BMRB Entry 16613

Name: SARS Coronavirus-unique domain (SUD): Three-domain molecular architecture in solution and RNA binding
Published: 2010-06-15

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16613

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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:

SARS Coronavirus-unique domain (SUD): Three-domain molecular architecture in solution and RNA binding

Deposition date:

2009-11-19

Original release date:

2010-06-15

Authors:

Johnson, Margaret; Chatterjee, Amarnath; Wuthrich, Kurt

Citation:

Citation: Johnson, Margaret; Chatterjee, Amarnath; Neuman, Benjamin; Wuthrich, Kurt. "SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding." J. Mol. Biol. 400, 724-742 (2010).
PubMed: 20493876

Assembly members:

Assembly members:
SUD-MC, polymer, 198 residues, Formula weight is not available

Natural source:

Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: Viruses 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-MC: GSHMGTVSWNLREMLAHAEE TRKLMPICMDVRAIMATIQR KYKGIKIQEGIVDYGVRFFF YTSKEPVASIITKLNSLNEP LVTMPIGYVTHGFNLEEAAR CMRSLKAPAVVSVSSPDAVT TYNGYLTSSSKTSEEHFVET VSLAGSYRDWSYSGQRTELG VEFLKRGDKIVYHTLESPVE FHLDGEVLSLDKLKSLLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	675
15N chemical shifts	201
1H chemical shifts	1407

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SUD-MC	1

Entities:

Entity 1, SUD-MC 198 residues - Formula weight is not available

Residues 1-4 represent a vector-derived tag. Residues 5-198 represent two domains of a multidomain protein. Residue 178 (PRO 700) is in cis conformation.

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

14

LYS

THR

SER

GLU

HIS

PHE

VAL

GLU

THR

15

VAL

SER

LEU

ALA

GLY

SER

TYR

ARG

ASP

TRP

16

SER

TYR

SER

GLY

GLN

ARG

THR

GLU

LEU

GLY

17

VAL

GLU

PHE

LEU

LYS

ARG

GLY

ASP

LYS

ILE

18

VAL

TYR

HIS

THR

LEU

GLU

SER

PRO

VAL

GLU

19

PHE

HIS

LEU

ASP

GLY

GLU

VAL

LEU

SER

LEU

20

ASP

LYS

LEU

LYS

SER

LEU

SER

Samples:

sample_1: SUD-MC, [U-98% 13C; U-98% 15N], 1.0 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.227 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D [15N,1H]-HSQC	sample_1	isotropic	sample_conditions_1
2D [13C,1H]-HSQC	sample_1	isotropic	sample_conditions_1
3D 15N-resolved [1H,1H-NOESY	sample_1	isotropic	sample_conditions_1
3D aliphatic 13C-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
4D APSY-HACANH	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-HNCOCA	sample_1	isotropic	sample_conditions_1
3D aromatic 13C-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

ASCAN, Fiorito F, Herrmann T, Damberger FF, Wuthrich K. - chemical shift assignment

MATCH, Volk, J., Herrmann, T., Wuthrich, K - chemical shift assignment

ATNOS, Herrmann T, Guntert P, Wuthrich K - peak picking

CANDID, Herrmann T, Guntert P, Wuthrich K - structure solution

OpalP, Luginbuhl P, Guntert P, Billeter M, Wuthrich K. - refinement

UNIO, Herrmann T, Wuthrich K - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	15469 15618
PDB	2JZD 2JZE 2JZF 2KQV 2KQW 2RNK 2W2G 2WCT
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