BMRB Entry 50300

Name: Sequence-specific resonance assignments of the Chlamydomonas reinhardtii SAS-6 N-terminal domain, F145E variant
Published: 2020-09-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50300

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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:

Sequence-specific resonance assignments of the Chlamydomonas reinhardtii SAS-6 N-terminal domain, F145E variant

Deposition date:

2020-05-28

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, 161 residues, Formula weight is not available

Natural source:

Natural source: Common Name: green algae Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Chlamydomonas reinhardtii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSTCm1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMPLLLDDGDPKAQTGFDL STATTLFWRPVPVHVKQQDR EDVLEELTFRILTGVAKQNH NLRILRIHISSDSDLFFLHT LEVSEEDFQSLKNDQGILVD FASFPGKIISLLEKCILAQP GDSPRFQAVLTIRGGESVFK IVEINDEKQLPHITLAFRPG N

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	410
15N chemical shifts	133
1H chemical shifts	133

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CrSAS-6N F145E	1

Entities:

Entity 1, CrSAS-6N F145E 161 residues - Formula weight is not available

First two residues are cloning artefact. E147 in assignment numbering is an engineered mutation.

1

GLY

PRO

MET

PRO

LEU

ASP

GLY

2

ASP

PRO

LYS

ALA

GLN

THR

GLY

PHE

ASP

LEU

3

SER

THR

ALA

THR

LEU

PHE

TRP

ARG

PRO

4

VAL

PRO

VAL

HIS

VAL

LYS

GLN

ASP

ARG

5

GLU

ASP

VAL

LEU

GLU

LEU

THR

PHE

ARG

6

ILE

LEU

THR

GLY

VAL

ALA

LYS

GLN

ASN

HIS

7

ASN

LEU

ARG

ILE

LEU

ARG

ILE

HIS

ILE

SER

8

SER

ASP

SER

ASP

LEU

PHE

LEU

HIS

THR

9

LEU

GLU

VAL

SER

GLU

ASP

PHE

GLN

SER

10

LEU

LYS

ASN

ASP

GLN

GLY

ILE

LEU

VAL

ASP

11

PHE

ALA

SER

PHE

PRO

GLY

LYS

ILE

SER

12

LEU

GLU

LYS

CYS

ILE

LEU

ALA

GLN

PRO

13

GLY

ASP

SER

PRO

ARG

PHE

GLN

ALA

VAL

LEU

14

THR

ILE

ARG

GLY

GLU

SER

VAL

PHE

LYS

15

ILE

VAL

GLU

ILE

ASN

ASP

GLU

LYS

GLN

LEU

16

PRO

HIS

ILE

THR

LEU

ALA

PHE

ARG

PRO

GLY

17

ASN

Samples:

sample_1: CrSAS-6N F145E, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; sodium phosphate 20 mM; D2O 5%; DSS 50 uM; 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 HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

SPARKY - data analysis

PIPP - data analysis

NMR spectrometers:

Bruker Avance II 500 MHz

UNP	A9CQL4
AlphaFold	A9CQL4