BMRB Entry 26793

Name: Backbone assignment of p24 GOLD domain
Published: 2016-10-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26793

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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:

Backbone assignment of p24 GOLD domain

Deposition date:

2016-05-10

Original release date:

2016-10-14

Authors:

Yamaguchi, Yoshiki; Nagae, Masamichi

Citation:

Citation: Nagae, Masamichi; Hirata, Tetsuya; Morita-Matsumoto, Kana; Theiler, Romina; Fujita, Morihisa; Kinoshita, Taroh; Yamaguchi, Yoshiki. "3D structure and interaction of p24beta and p24delta Golgi dynamics domains: implications for p24 complex formation and cargo transport" J. Mol. Biol. 428, 4087-4099 (2016).
PubMed: 27569046

Assembly members:

Assembly members:
p24, polymer, 101 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p24: GSSGYFVSIDAHAEECFFER VTSGTKMGLIFEVAEGGFLD IDVEITGPDNKGIYKGDRES SGKYTFAAHMDGTYKFCFSN RMSTMTPKIVMFTIDIGEAP K

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	85
15N chemical shifts	48
1H chemical shifts	48

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GOLD domain	1

Entities:

Entity 1, GOLD domain 101 residues - Formula weight is not available

1

GLY

SER

GLY

TYR

PHE

VAL

SER

ILE

ASP

2

ALA

HIS

ALA

GLU

CYS

PHE

GLU

ARG

3

VAL

THR

SER

GLY

THR

LYS

MET

GLY

LEU

ILE

4

PHE

GLU

VAL

ALA

GLU

GLY

PHE

LEU

ASP

5

ILE

ASP

VAL

GLU

ILE

THR

GLY

PRO

ASP

ASN

6

LYS

GLY

ILE

TYR

LYS

GLY

ASP

ARG

GLU

SER

7

SER

GLY

LYS

TYR

THR

PHE

ALA

HIS

MET

8

ASP

GLY

THR

TYR

LYS

PHE

CYS

PHE

SER

ASN

9

ARG

MET

SER

THR

MET

THR

PRO

LYS

ILE

VAL

10

MET

PHE

THR

ILE

ASP

ILE

GLY

GLU

ALA

PRO

11

LYS

Samples:

sample_1: p24, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O 10%; sodium phosphate 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 600 MHz

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