BMRB Entry 51397

Name: Mouse complexin-1 C-terminal domain + DPC micelles chemical shift information
Published: 2022-07-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51397

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Mouse complexin-1 C-terminal domain + DPC micelles chemical shift information PubMed: 35777466

Deposition date: 2022-04-08 Original release date: 2022-07-06

Authors: Grasso, Emily; Terakawa, Mayu; Lai, Alex; Xue Xie, Ying; Ramlall, Trudy; Freed, Jack; Eliezer, David

Citation: Grasso, Emily; Terakawa, Mayu; Lai, Alex; Xue Xie, Ying; Ramlall, Trudy; Freed, Jack; Eliezer, David. "Membrane binding induces distinct structural signatures in the mouse complexin-1 C-terminal domain" J. Mol. Biol. 435, 167710-167710 (2023).

Assembly members:
entity_1, polymer, 64 residues, Formula weight is not available

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity_1: GIKKKEEREAEAQAAMEANS EGSLTRPKKAIPPGCGDEPE EEDESILDTVIKYLPGPLQD MFKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	173
15N chemical shifts	56
1H chemical shifts	56

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mCpx1 CTD, 1	1
2	mCpx1 CTD, 2	1

Entities:

Entity 1, mCpx1 CTD, 1 64 residues - Formula weight is not available

1

GLY

ILE

LYS

GLU

ARG

GLU

ALA

2

GLU

ALA

GLN

ALA

MET

GLU

ALA

ASN

SER

3

GLU

GLY

SER

LEU

THR

ARG

PRO

LYS

ALA

4

ILE

PRO

GLY

CYS

GLY

ASP

GLU

PRO

GLU

5

GLU

ASP

GLU

SER

ILE

LEU

ASP

THR

VAL

6

ILE

LYS

TYR

LEU

PRO

GLY

PRO

LEU

GLN

ASP

7

MET

PHE

LYS

Samples:

sample_1: Mouse complexin-1 CTD, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; EDTA 0.5 mM; 2H DPC, [U-2H], 60 mM

sample_conditions_1: ionic strength: 0.408 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(COCA)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - data analysis

NMRbox - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

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