BMRB Entry 50003

Name: EB3 200-281 NMR chemical shift assignments
Published: 2020-04-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50003

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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:

EB3 200-281 NMR chemical shift assignments

Deposition date:

2019-08-20

Original release date:

2020-04-17

Authors:

Gaponenko, Vadim; Komarova, Yulia; Hitchinson, Ben

Citation:

Citation: Abdelkarim, Hazem; Hitchinson, Ben; Qu, Xinyan; Banerjee, Avik; Komarova, Yulia; Gaponenko, Vadim. "NMR Resonance Assignment and Structure Prediction of the C-terminal Domain of the Microtubule End-Binding Protein 3" PLOS ONE 15, e0232338-e0232338 (2020).
PubMed: 32421702

Assembly members:

Assembly members:
entity_1, polymer, 82 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: PET42a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AQILELNQQLVDLKLTVDGL EKERDFYFSKLRDIELICQE HESENSPVISGIIGILYATE EGFAPPEDDEIEEHQQEDQD EY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	119
15N chemical shifts	74
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EB3 C-term	1

Entities:

Entity 1, EB3 C-term 82 residues - Formula weight is not available

1

ALA

GLN

ILE

LEU

GLU

LEU

ASN

GLN

LEU

2

VAL

ASP

LEU

LYS

LEU

THR

VAL

ASP

GLY

LEU

3

GLU

LYS

GLU

ARG

ASP

PHE

TYR

PHE

SER

LYS

4

LEU

ARG

ASP

ILE

GLU

LEU

ILE

CYS

GLN

GLU

5

HIS

GLU

SER

GLU

ASN

SER

PRO

VAL

ILE

SER

6

GLY

ILE

GLY

ILE

LEU

TYR

ALA

THR

GLU

7

GLU

GLY

PHE

ALA

PRO

GLU

ASP

GLU

8

ILE

GLU

HIS

GLN

GLU

ASP

GLN

ASP

9

GLU

TYR

Samples:

sample_1: EB3 C-term, [U-100% 13C; U-100% 15N], 350 uM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz

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