BMRB Entry 27107

Name: Backbone and beta carbon 1H, 13C, and 15N chemical shift assignments for the worm complexin-1 CTD in the presence of dodecylphosphocholine micelles
Published: 2021-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27107

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 and beta carbon 1H, 13C, and 15N chemical shift assignments for the worm complexin-1 CTD in the presence of dodecylphosphocholine micelles PubMed: 28596722

Deposition date: 2017-05-15 Original release date: 2021-07-22

Authors: Snead, David; Eliezer, David

Citation: Snead, David; Lai, Alex; Wragg, Rachel; Parisotto, Daniel; Ramlall, Trudy; Dittman, Jeremy; Freed, Jack; Eliezer, David. "Unique Structural Features of Membrane-Bound C-Terminal Domain Motifs Modulate Complexin Inhibitory Function" Front Mol. Neurosci. 10, 154-154 (2017).

Assembly members:
complexin-1_C-terminal_domain, polymer, 53 residues, Formula weight is not available

Natural source: Common Name: C. elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

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

Entity Sequences (FASTA):
complexin-1_C-terminal_domain: GGPRKTPEEIAAEMNAEDDS LIGQLGLTEQVEKAKTMATG AFETVKGFFPFGK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	148
15N chemical shifts	48
1H chemical shifts	48

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	complexin-1 C-terminal domain	1

Entities:

Entity 1, complexin-1 C-terminal domain 53 residues - Formula weight is not available

1

GLY

PRO

ARG

LYS

THR

PRO

GLU

ILE

2

ALA

GLU

MET

ASN

ALA

GLU

ASP

SER

3

LEU

ILE

GLY

GLN

LEU

GLY

LEU

THR

GLU

GLN

4

VAL

GLU

LYS

ALA

LYS

THR

MET

ALA

THR

GLY

5

ALA

PHE

GLU

THR

VAL

LYS

GLY

PHE

PRO

6

PHE

GLY

LYS

Samples:

sample_1: complexin-1 C-terminal domain, [U-13C; U-15N; U-2H], 650 uM

sample_conditions_1: ionic strength: 0.11 M; pH: 6.1; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Bruker Avance 900 MHz
Varian INOVA 600 MHz

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