BMRB Entry 50308

Name: Sequence-specific resonance assignments of the human SAS-6 F131D head domain
Published: 2020-09-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50308

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:

Sequence-specific resonance assignments of the human SAS-6 F131D head domain

Deposition date:

2020-06-07

Original release date:

2020-09-01

Authors:

Busch, Julia; Vakonakis, Ioannis

Citation:

Citation: Busch, Julia; Matsoukas, Minos-Timotheos; Musgaard, Maria; Spyroulias, Georgios; Biggin, Philip; Vakonakis, Ioannis. "Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerization" J. Biol. Chem. 295, 17922-17934 (2020).
PubMed: 32873708

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, Formula weight is not available

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: pFLOAT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMSQVLFHQLVPLQVKCKD CEERRVSIRMSIELQSVSNP VHRKDLVIRLTDDTDPFFLY NLVISEEDFQSLKFQQGLLV DFLAFPQKFIDLLQQCTQEH AKEIPRFLLQLVSPAAILDN SPAFLNVVETNPDKHLTHLS LKLLPGNDVEIKKF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	224
15N chemical shifts	110
1H chemical shifts	110

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hsSAS-6	1

Entities:

Entity 1, hsSAS-6 154 residues - Formula weight is not available

First two residues are cloning artifacts

1

GLY

PRO

MET

SER

GLN

VAL

LEU

PHE

HIS

GLN

2

LEU

VAL

PRO

LEU

GLN

VAL

LYS

CYS

LYS

ASP

3

CYS

GLU

ARG

VAL

SER

ILE

ARG

MET

4

SER

ILE

GLU

LEU

GLN

SER

VAL

SER

ASN

PRO

5

VAL

HIS

ARG

LYS

ASP

LEU

VAL

ILE

ARG

LEU

6

THR

ASP

THR

ASP

PRO

PHE

LEU

TYR

7

ASN

LEU

VAL

ILE

SER

GLU

ASP

PHE

GLN

8

SER

LEU

LYS

PHE

GLN

GLY

LEU

VAL

9

ASP

PHE

LEU

ALA

PHE

PRO

GLN

LYS

PHE

ILE

10

ASP

LEU

GLN

CYS

THR

GLN

GLU

HIS

11

ALA

LYS

GLU

ILE

PRO

ARG

PHE

LEU

GLN

12

LEU

VAL

SER

PRO

ALA

ILE

LEU

ASP

ASN

13

SER

PRO

ALA

PHE

LEU

ASN

VAL

GLU

THR

14

ASN

PRO

ASP

LYS

HIS

LEU

THR

HIS

LEU

SER

15

LEU

LYS

LEU

PRO

GLY

ASN

ASP

VAL

GLU

16

ILE

LYS

PHE

Samples:

sample_1: hsSAS-6, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 5%; DSS 50 uM; sodium chloride 150 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.38 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN - collection

NMRPipe - processing

SPARKY - data analysis

PINE - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 17.6 MHz

UNP	Q6UVJ0
AlphaFold	Q8N3K0