BMRB Entry 52661

Name: Chemical shift assignment of human recombinant DN-CyPD
Published: 2024-12-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52661

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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:

Chemical shift assignment of human recombinant DN-CyPD

Deposition date:

2024-10-25

Original release date:

2024-12-11

Authors:

Coluccino, Gabriele; Corazza, Alessandra

Citation:

Citation: Coluccino, Gabriele; Negro, Alessandro; Filippi, Antonio; Bean, Camilla; Muraca, Valentina Pia; Gissi, Clarissa; Canetti, Diana; Mimmi, Maria Chiara; Zamprogno, Elisa; Ciscato, Francesco; Acquasaliente, Laura; De Filippis, Vincenzo; Comelli, Marina; Carraro, Michela; Rasola, Andrea; Gerle, Christoph; Bernardi, Paolo; Corazza, Alessandra; Lippe, Giovanna. "N-terminal cleavage of cyclophilin D boosts its ability to bind F-ATP synthase" Commun. Biol. 7, 1486-1486 (2024).
PubMed: 39528709

Assembly members:

Assembly members:
entity_1, polymer, 165 residues, 17643.13 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGNPLVYLDVDANGKPLGRV VLELKADVVPKTAENFRALC TGEKGFGYKGSTFHRVIPSF MCQAGDFTNHNGTGGKSIYG SRFPDENFTLKHVGPGVLSM ANAGPNTNGSQFFICTIKTD WLDGKHVVFGHVKEGMDVVK KIESFGSKSGRTSKKIVITD CGQLS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	461
15N chemical shifts	152
1H chemical shifts	152

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CyPD	1

Entities:

Entity 1, CyPD 165 residues - 17643.13 Da.

Residue numbering was kept the same as FL-CyPD, i.e., parental protein from which DN-CyPD is generated.

1

SER

GLY

ASN

PRO

LEU

VAL

TYR

LEU

ASP

VAL

2

ASP

ALA

ASN

GLY

LYS

PRO

LEU

GLY

ARG

VAL

3

VAL

LEU

GLU

LEU

LYS

ALA

ASP

VAL

PRO

4

LYS

THR

ALA

GLU

ASN

PHE

ARG

ALA

LEU

CYS

5

THR

GLY

GLU

LYS

GLY

PHE

GLY

TYR

LYS

GLY

6

SER

THR

PHE

HIS

ARG

VAL

ILE

PRO

SER

PHE

7

MET

CYS

GLN

ALA

GLY

ASP

PHE

THR

ASN

HIS

8

ASN

GLY

THR

GLY

LYS

SER

ILE

TYR

GLY

9

SER

ARG

PHE

PRO

ASP

GLU

ASN

PHE

THR

LEU

10

LYS

HIS

VAL

GLY

PRO

GLY

VAL

LEU

SER

MET

11

ALA

ASN

ALA

GLY

PRO

ASN

THR

ASN

GLY

SER

12

GLN

PHE

ILE

CYS

THR

ILE

LYS

THR

ASP

13

TRP

LEU

ASP

GLY

LYS

HIS

VAL

PHE

GLY

14

HIS

VAL

LYS

GLU

GLY

MET

ASP

VAL

LYS

15

LYS

ILE

GLU

SER

PHE

GLY

SER

LYS

SER

GLY

16

ARG

THR

SER

LYS

ILE

VAL

ILE

THR

ASP

17

CYS

GLY

GLN

LEU

SER

Samples:

sample_1: Cyclophilin D, [U-100% 13C; U-100% 15N], 400 uM; DTT 20 mM; NaPi 20 mM; DTE 2 mM

sample_conditions_1: pH: 7.00; pressure: 1 atm; temperature: 298 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.190 - chemical shift assignment

NMRFAM-SPARKY v3.190 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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