BMRB Entry 52551

Name: Human CHCHD2 N-Terminus
Published: 2024-08-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52551

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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:

Human CHCHD2 N-Terminus

Deposition date:

2024-07-15

Original release date:

2024-08-15

Authors:

Mancinelli, Chiara; Lv, Guohua; Sayles, Nicoles; Huang, Yun; McAvoy, Kevin; Manfredi, Giovanni; Fujita, Hibiki; Eliezer, David

Citation:

Citation: Lv, Guohua; Sayles, Nicole; Huang, Yun; Mancinelli, Chiara; McAvoy, Kevin; Shneider, Neil; Manfredi, Giovanni; Kawamata, Hibiki; Eliezer, David. "Amyloid fibril structures link CHCHD10 and CHCHD2 to neurodegeneration" bioRxiv ., .-. (2024).
PubMed: 39091724

Assembly members:

Assembly members:
entity_1, polymer, 114 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-28(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPRGSRSRTSRMAPPASRAP QMRAAPRPAPVAQPPAAAPP SAVGSSAAAPRQPGLMAQMA TTAAGVAVGSAVGHTLGHAI TGGFSGGSNAEPARPDITYQ EPQGTQPAQQQQPM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	305
15N chemical shifts	93
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hCHCHD2_NTerm	1

Entities:

Entity 1, hCHCHD2_NTerm 114 residues - Formula weight is not available

1

MET

PRO

ARG

GLY

SER

ARG

SER

ARG

THR

SER

2

ARG

MET

ALA

PRO

ALA

SER

ARG

ALA

PRO

3

GLN

MET

ARG

ALA

PRO

ARG

PRO

ALA

PRO

4

VAL

ALA

GLN

PRO

ALA

PRO

5

SER

ALA

VAL

GLY

SER

ALA

PRO

6

ARG

GLN

PRO

GLY

LEU

MET

ALA

GLN

MET

ALA

7

THR

ALA

GLY

VAL

ALA

VAL

GLY

SER

8

ALA

VAL

GLY

HIS

THR

LEU

GLY

HIS

ALA

ILE

9

THR

GLY

PHE

SER

GLY

SER

ASN

ALA

10

GLU

PRO

ALA

ARG

PRO

ASP

ILE

THR

TYR

GLN

11

GLU

PRO

GLN

GLY

THR

GLN

PRO

ALA

GLN

12

GLN

PRO

MET

Samples:

sample_1: hCHCHD2_NTerm, [U-100% 13C; U-100% 15N], 200 uM; D2O 10%; H2O 90%; sodium chloride 100 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 283 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

SPARKY - data analysis

NMRbox - data analysis

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 800 MHz

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