BMRB Entry 26792

Name: Backbone assignment of p23 GOLD domain
Published: 2016-10-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26792

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone assignment of p23 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:
p23, polymer, 103 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):
p23: GSISFHLPVNSRKCLREEIH KDLLVTGAYEITDQSGGAGG LRTHLKITDSAGHILYAKED ATKGKFAFTTEDYDMFEVCF ESKGTGRIPDQLVILDMKHG VEA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	162
15N chemical shifts	81
1H chemical shifts	81

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GOLD domain	1

Entities:

Entity 1, GOLD domain 103 residues - Formula weight is not available

1

GLY

SER

ILE

SER

PHE

HIS

LEU

PRO

VAL

ASN

2

SER

ARG

LYS

CYS

LEU

ARG

GLU

ILE

HIS

3

LYS

ASP

LEU

VAL

THR

GLY

ALA

TYR

GLU

4

ILE

THR

ASP

GLN

SER

GLY

ALA

GLY

5

LEU

ARG

THR

HIS

LEU

LYS

ILE

THR

ASP

SER

6

ALA

GLY

HIS

ILE

LEU

TYR

ALA

LYS

GLU

ASP

7

ALA

THR

LYS

GLY

LYS

PHE

ALA

PHE

THR

8

GLU

ASP

TYR

ASP

MET

PHE

GLU

VAL

CYS

PHE

9

GLU

SER

LYS

GLY

THR

GLY

ARG

ILE

PRO

ASP

10

GLN

LEU

VAL

ILE

LEU

ASP

MET

LYS

HIS

GLY

11

VAL

GLU

ALA

Samples:

sample_1: p23, [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