BMRB Entry 27767

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for bacteriophage protein Gp46
Published: 2019-03-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27767

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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for bacteriophage protein Gp46

Deposition date:

2019-01-26

Original release date:

2019-03-08

Authors:

Liu, Bing

Citation:

Citation: Zhang, Peipei; Wang, Zhihao; Zhao, Siyu; Wang, Yawen; Matthews, Steve; Liu, Bing. "1H, 13C and 15N NMR assignments of Bacillus subtilis bacteriophage SPO1 protein Gp46" Biomol. NMR Assignments 13, 245-247 (2019).
PubMed: 30830594

Assembly members:

Assembly members:
Gp46, polymer, 77 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Gp46: MMTEDQKFKYLTKIEELEAG CFSDWTKEDITGDLKYLKKG IIEESIELIRAVNGLTYSEE LHDFTQEIIEELDISPL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	355
15N chemical shifts	76
1H chemical shifts	558

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Gp46	1

Entities:

Entity 1, Gp46 77 residues - Formula weight is not available

1

MET

THR

GLU

ASP

GLN

LYS

PHE

LYS

TYR

2

LEU

THR

LYS

ILE

GLU

LEU

GLU

ALA

GLY

3

CYS

PHE

SER

ASP

TRP

THR

LYS

GLU

ASP

ILE

4

THR

GLY

ASP

LEU

LYS

TYR

LEU

LYS

GLY

5

ILE

GLU

SER

ILE

GLU

LEU

ILE

ARG

6

ALA

VAL

ASN

GLY

LEU

THR

TYR

SER

GLU

7

LEU

HIS

ASP

PHE

THR

GLN

GLU

ILE

GLU

8

GLU

LEU

ASP

ILE

SER

PRO

LEU

Samples:

sample_1: Gp46, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 300 mM; TCEP 1 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 0.35 M; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - chemical shift assignment, processing

NMR spectrometers:

Bruker Avance 600 MHz

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