BMRB Entry 7218

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7218

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 13C and 15N assignment of the Master-Rep protein nuclease domain from the Faba Bean Necrotic Yellows Virus

Deposition date:

2006-07-10

Original release date:

2006-10-30

Authors:

Vega-Rocha, Susana; Campos-Olivas, Ramon

Citation:

Citation: Vega-Rocha, Susana; Gronenborn, A.; Gronenborn, B.; Campos-Olivas, Ramon. "(1)H, (13)C, and (15)N NMR assignment of the master Rep protein nuclease domain from the Nanovirus FBNYV" J. Biomol. NMR 38, 169-169 (2007).
PubMed: 17043745

Assembly members:

Assembly members:
N-terminal DNA binding domain of M-Rep protein from the nanovirus FBNYV, polymer, 138 residues, 15866.0 Da.

Natural source:

Natural source: Common Name: Faba Bean Necrotic Yellows Virus Taxonomy ID: 59817 Superkingdom: Viruses Kingdom: Viridiplantae Genus/species: Nanovirus Faba Bean Necrotic Yellows Virus

Experimental source:

Experimental source: Production method: recombinant technology Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal DNA binding domain of M-Rep protein from the nanovirus FBNYV: GSSHHHHHHSSGLEVLFQGP HMARQVICWCFTLNNPLSPL SLHDSMKYLVYQTEQGEAGN IHFQGYIEMKKRTSLAGMKK LIPGAHFEKRRGTQGEARAY SMKEDTRLEGPWEYGEFVPT IEDKLREVMNDMKITGKR

Data sets:

assigned_chemical_shifts
- chem_shift_list_1
coupling_constants
- J_coupling_list_1

Data type	Count
13C chemical shifts	356
15N chemical shifts	127
1H chemical shifts	559
coupling constants	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	monomer	1

Entities:

Entity 1, monomer 138 residues - 15866.0 Da.

1

GLY

SER

HIS

SER

2

SER

GLY

LEU

GLU

VAL

LEU

PHE

GLN

GLY

PRO

3

HIS

MET

ALA

ARG

GLN

VAL

ILE

CYS

TRP

CYS

4

PHE

THR

LEU

ASN

PRO

LEU

SER

PRO

LEU

5

SER

LEU

HIS

ASP

SER

MET

LYS

TYR

LEU

VAL

6

TYR

GLN

THR

GLU

GLN

GLY

GLU

ALA

GLY

ASN

7

ILE

HIS

PHE

GLN

GLY

TYR

ILE

GLU

MET

LYS

8

LYS

ARG

THR

SER

LEU

ALA

GLY

MET

LYS

9

LEU

ILE

PRO

GLY

ALA

HIS

PHE

GLU

LYS

ARG

10

ARG

GLY

THR

GLN

GLY

GLU

ALA

ARG

ALA

TYR

11

SER

MET

LYS

GLU

ASP

THR

ARG

LEU

GLU

GLY

12

PRO

TRP

GLU

TYR

GLY

GLU

PHE

VAL

PRO

THR

13

ILE

GLU

ASP

LYS

LEU

ARG

GLU

VAL

MET

ASN

14

ASP

MET

LYS

ILE

THR

GLY

LYS

ARG

Samples:

sample_1: FBNYV M-Rep (1-117), [U-10% 13C; U-15N], 0.4; Sodium phosphate 20; NaCl 600; DTT 1; D2O 8%

sample_2: FBNYV M-Rep (1-117), [U-13C; U-15N], 0.4; Sodium phosphate 20; NaCl 600; DTT 1; D2O 8%

conditions_1: ionic strength: 1.264 M; pH: 6.6; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H15N_HSQC	not available	not available	conditions_1
3D HNCO	not available	not available	conditions_1
3D HNCACB	not available	not available	conditions_1
3D CBCA (CO) NH	not available	not available	conditions_1
3D HNHA	not available	not available	conditions_1
3D 15N edited NOESY	not available	not available	conditions_1
3D CC (CO) NH	not available	not available	conditions_1
3D 15N edited TOCSY	not available	not available	conditions_1

Software:

NMRPipe v97.027.12.56 -

NMRView v5.0.20 -

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	7112
PDB	2HWT
EMBL	CAA72209 CAB44020
GB	ACX50503
REF	NP_619567
SP	O39828 Q9WIJ5
AlphaFold	O39828 Q9WIJ5