BMRB Entry 27406

Name: Backbone and side chain NMR assignments for heterologously expressed Er-23
Published: 2018-06-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27406

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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:

Backbone and side chain NMR assignments for heterologously expressed Er-23

Deposition date:

2018-02-18

Original release date:

2018-06-20

Authors:

Bowles, David; Hansen, Alexandar; Rhoads, Calvin; Yuan, Chunhua; Magliery, Thomas

Citation:

Citation: Bowles, David; Hansen, Alexandar; Rhoads, Calvin; Yuan, Chunhua; Magliery, Thomas. "1H, 13C, 15N resonance assignment of recombinant Euplotes raikovi protein Er-23" Biomol. NMR Assignments 12, 291-295 (2018).
PubMed: 29876749

Assembly members:

Assembly members:
Er-23, polymer, 54 residues, 5300 Da.

Natural source:

Natural source: Common Name: Euplotes raikovi Taxonomy ID: 5938 Superkingdom: Eukaryota Kingdom: Ciliophora Genus/species: Euplotes raikovi

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Er-23: GSSGECEQCFSDGGDCTTCF NNGTGPCANCLAGYPAGCSN SDCTAFLSQCYGGC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	112
15N chemical shifts	56
1H chemical shifts	249

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Er-23	1

Entities:

Entity 1, Er-23 54 residues - 5300 Da.

1

GLY

SER

GLY

GLU

CYS

GLU

GLN

CYS

PHE

2

SER

ASP

GLY

ASP

CYS

THR

CYS

PHE

3

ASN

GLY

THR

GLY

PRO

CYS

ALA

ASN

CYS

4

LEU

ALA

GLY

TYR

PRO

ALA

GLY

CYS

SER

ASN

5

SER

ASP

CYS

THR

ALA

PHE

LEU

SER

GLN

CYS

6

TYR

GLY

CYS

Samples:

sample_1: Er-23, [U-100% 13C; U-100% 15N], 1 – 1.2 mM; Tris-HCl1 – 50 mM; Tris-HCl1 – 300 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Ascend 700 MHz

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