BMRB Entry 51533

Name: Sequential NMR assignment of human protein DPCD
Published: 2022-08-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51533

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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:

Sequential NMR assignment of human protein DPCD

Deposition date:

2022-07-26

Original release date:

2022-08-02

Authors:

Schelcher, Cedric; Morellet, Nelly; Quinternet, Marc; Manival, Xavier

Citation:

Citation: Morais, Raphael Dos Santos; Santo, Paulo Espirito; Ley, Marie; Schelcher, Cedric; Abel, Yoann; Plassart, Laura; Desligniere, Evolene; Chagot, Marie-Eve; Quinternet, Marc; Paiva, Ana C.F.; Hessmann, Steve; Morellet, Nelly; Sousa, Pedro M. F.; Vandermoere, Franck; Bertrand, Edouard; Charpentier, Bruno; Bandeiras, Tiago M.; Plisson-Chastang, Celia; Verheggen, Celine; Cianferani, Sarah; Manival, Xavier. "Deciphering cellular and molecular determinants of human DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases" J. Mol. Biol. 434, 167760-167760 (2022).
PubMed: 35901867

Assembly members:

Assembly members:
entity_1, polymer, 206 residues, 23531 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: pnEA3CH

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMAVTGWLESLRTAQKTA LLQDGRRKVHYLFPDGKEMA EEYDEKTSELLVRKWRVKSA LGAMGQWQLEVGDPAPLGAG NLGPELIKESNANPIFMRKD TKMSFQWRIRNLPYPKDVYS VSVDQKERCIIVRTTNKKYY KKFSIPDLDRHQLPLDDASL SFAHANCTLIISYQKPKEVV VAESELQKELKKVKTAHSND GDCKTQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	440
15N chemical shifts	157
1H chemical shifts	157

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DPCD	1

Entities:

Entity 1, DPCD 206 residues - 23531 Da.

206 residues

1

GLY

PRO

HIS

MET

ALA

VAL

THR

GLY

TRP

LEU

2

GLU

SER

LEU

ARG

THR

ALA

GLN

LYS

THR

ALA

3

LEU

GLN

ASP

GLY

ARG

LYS

VAL

HIS

4

TYR

LEU

PHE

PRO

ASP

GLY

LYS

GLU

MET

ALA

5

GLU

TYR

ASP

GLU

LYS

THR

SER

GLU

LEU

6

LEU

VAL

ARG

LYS

TRP

ARG

VAL

LYS

SER

ALA

7

LEU

GLY

ALA

MET

GLY

GLN

TRP

GLN

LEU

GLU

8

VAL

GLY

ASP

PRO

ALA

PRO

LEU

GLY

ALA

GLY

9

ASN

LEU

GLY

PRO

GLU

LEU

ILE

LYS

GLU

SER

10

ASN

ALA

ASN

PRO

ILE

PHE

MET

ARG

LYS

ASP

11

THR

LYS

MET

SER

PHE

GLN

TRP

ARG

ILE

ARG

12

ASN

LEU

PRO

TYR

PRO

LYS

ASP

VAL

TYR

SER

13

VAL

SER

VAL

ASP

GLN

LYS

GLU

ARG

CYS

ILE

14

ILE

VAL

ARG

THR

ASN

LYS

TYR

15

LYS

PHE

SER

ILE

PRO

ASP

LEU

ASP

ARG

16

HIS

GLN

LEU

PRO

LEU

ASP

ALA

SER

LEU

17

SER

PHE

ALA

HIS

ALA

ASN

CYS

THR

LEU

ILE

18

ILE

SER

TYR

GLN

LYS

PRO

LYS

GLU

VAL

19

VAL

ALA

GLU

SER

GLU

LEU

GLN

LYS

GLU

LEU

20

LYS

VAL

LYS

THR

ALA

HIS

SER

ASN

ASP

21

GLY

ASP

CYS

LYS

THR

GLN

Samples:

sample_1: DPCD, [U-100% 13C; U-100% 15N], 1.8 ± 0.35 mM; NaPi 10 mM; NaCl 300 mM; DTT deuterated 5 mM

sample_2: DPCD, [U-100% 13C; U-100% 15N; U-80% 2H], 1.3 ± 0.25 mM; NaPi 10 mM; NaCl 300 mM; DTT deuterated 5 mM

sample_conditions_1: ionic strength: 310 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCACONH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCACONH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN vversion 3.0 - collection

CARA v1.9.1 - chemical shift assignment

TALOS-N v4.12 - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 950 MHz

UNP	Q9BVM2
AlphaFold	Q9UFY6