BMRB Entry 52665

Name: Chemical shift assignment of human recombinant mature CyPD (FL-CyPD)
Published: 2024-12-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52665

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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 mature CyPD (FL-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, 178 residues, 18897.38 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: CSKGSGDPSSSSSSGNPLVY LDVDANGKPLGRVVLELKAD VVPKTAENFRALCTGEKGFG YKGSTFHRVIPSFMCQAGDF TNHNGTGGKSIYGSRFPDEN FTLKHVGPGVLSMANAGPNT NGSQFFICTIKTDWLDGKHV VFGHVKEGMDVVKKIESFGS KSGRTSKKIVITDCGQLS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	475
15N chemical shifts	158
1H chemical shifts	158

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FL-CyPD	1

Entities:

Entity 1, FL-CyPD 178 residues - 18897.38 Da.

1

CYS

SER

LYS

GLY

SER

GLY

ASP

PRO

SER

2

SER

GLY

ASN

PRO

LEU

VAL

TYR

3

LEU

ASP

VAL

ASP

ALA

ASN

GLY

LYS

PRO

LEU

4

GLY

ARG

VAL

LEU

GLU

LEU

LYS

ALA

ASP

5

VAL

PRO

LYS

THR

ALA

GLU

ASN

PHE

ARG

6

ALA

LEU

CYS

THR

GLY

GLU

LYS

GLY

PHE

GLY

7

TYR

LYS

GLY

SER

THR

PHE

HIS

ARG

VAL

ILE

8

PRO

SER

PHE

MET

CYS

GLN

ALA

GLY

ASP

PHE

9

THR

ASN

HIS

ASN

GLY

THR

GLY

LYS

SER

10

ILE

TYR

GLY

SER

ARG

PHE

PRO

ASP

GLU

ASN

11

PHE

THR

LEU

LYS

HIS

VAL

GLY

PRO

GLY

VAL

12

LEU

SER

MET

ALA

ASN

ALA

GLY

PRO

ASN

THR

13

ASN

GLY

SER

GLN

PHE

ILE

CYS

THR

ILE

14

LYS

THR

ASP

TRP

LEU

ASP

GLY

LYS

HIS

VAL

15

VAL

PHE

GLY

HIS

VAL

LYS

GLU

GLY

MET

ASP

16

VAL

LYS

ILE

GLU

SER

PHE

GLY

SER

17

LYS

SER

GLY

ARG

THR

SER

LYS

ILE

VAL

18

ILE

THR

ASP

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