BMRB Entry 34925

Name: Structure of the ASH1 domain of Drosophila melanogaster Spd-2
Published: 2025-03-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34925

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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:

Structure of the ASH1 domain of Drosophila melanogaster Spd-2

Deposition date:

2024-06-26

Original release date:

2025-03-26

Authors:

Sheppard, D.; Feng, Z.; Lea, S.; Johnson, S.; Raff, J.

Citation:

Citation: Hu, Liuyi; Wainman, Alan; Andreeva, Antonina; Apizi, Muladili; Alvarez-Rodrigo, Ines; Wong, Siu-Shing; Saurya, Saroj; Sheppard, Devon; Cottee, Matthew; Johnson, Steven; Lea, Susan; Raff, Jordan; van Breugel, Mark; Feng, Zhe. "The conserved Spd-2/CEP192 domain adopts a unique protein fold to promote centrosome scaffold assembly" Sci. Adv. 11, eadr5744-eadr5744 (2025).
PubMed: 40106572

Assembly members:

Assembly members:
entity_1, polymer, 113 residues, 11960.872 Da.

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMGLLPLKVTHTTLCWGST KLRTDVRKSMQVKNTADKRL VIRLGIQGPGFQLVGTDSST ITLQAMECRSVVINFCPTVC GAAIGALSFYAPPGAHNSNQ PGLEIPLYGYGGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	475
15N chemical shifts	110
1H chemical shifts	706

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 113 residues - 11960.872 Da.

1

GLY

PRO

MET

GLY

LEU

PRO

LEU

LYS

VAL

2

THR

HIS

THR

LEU

CYS

TRP

GLY

SER

THR

3

LYS

LEU

ARG

THR

ASP

VAL

ARG

LYS

SER

MET

4

GLN

VAL

LYS

ASN

THR

ALA

ASP

LYS

ARG

LEU

5

VAL

ILE

ARG

LEU

GLY

ILE

GLN

GLY

PRO

GLY

6

PHE

GLN

LEU

VAL

GLY

THR

ASP

SER

THR

7

ILE

THR

LEU

GLN

ALA

MET

GLU

CYS

ARG

SER

8

VAL

ILE

ASN

PHE

CYS

PRO

THR

VAL

CYS

9

GLY

ALA

ILE

GLY

ALA

LEU

SER

PHE

TYR

10

ALA

PRO

GLY

ALA

HIS

ASN

SER

ASN

GLN

11

PRO

GLY

LEU

GLU

ILE

PRO

LEU

TYR

GLY

TYR

12

GLY

SER

Samples:

sample_1: Na2HPO4 100 mM; NaCl 137 mM; KCl 27 mM; KH2PO4 18 mM; ZnCl2 1 uM; DTT 1 mM; Spd-2, [U-13C; U-15N], 0.5 mM

sample_conditions_1: ionic strength: 0.196 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CCCONH	sample_1	isotropic	sample_conditions_1
3D HCCCONH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRFAM-SPARKY, Shin J, Lee W, Lee W. - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE II 500 MHz
Bruker AVANCE II 600 MHz

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