BMRB Entry 51747

Name: Backbone Assignment of the S519N variant of SASH1 Pigmentation Associated Disordered Region (SPIDER)
Published: 2023-04-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51747

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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 the S519N variant of SASH1 Pigmentation Associated Disordered Region (SPIDER)

Deposition date:

2022-12-19

Original release date:

2023-04-21

Authors:

Clements, Christopher; Shellman, Yiqun; Vogeli, Beat; Henen, Morkos

Citation:

Citation: Clements, Christopher; Shellman, Yiqun; Vogeli, Beat; Henen, Morkos. "Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER)" Biomol. NMR Assign. 17, 151-157 (2023).
PubMed: 37155029

Assembly members:

Assembly members:
entity_1, polymer, 169 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: Pet28 a (+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GLGSLSHGRTCSFGGFDLTN RSLHVGSNNSDPMGKEGDFV YKEVIKSPTASRISLGKKVK SVKETMRKRMSKKYSSSVSE QDSGLDGMPGSPPPSQPDPE HLDKPKLKAGGSVESLRSSL SGQNSMSGQTVSTTDSSTSN RESVKSEDGDDEEPPYRGPF CGRARVHTD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	460
15N chemical shifts	153
1H chemical shifts	153

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SPIDER-SASH1	1

Entities:

Entity 1, SPIDER-SASH1 169 residues - Formula weight is not available

SASH1 396-564 (Linker: 396-400, SPIDER: 401-553 & SH3: 554-564)

1

GLY

LEU

GLY

SER

LEU

SER

HIS

GLY

ARG

THR

2

CYS

SER

PHE

GLY

PHE

ASP

LEU

THR

ASN

3

ARG

SER

LEU

HIS

VAL

GLY

SER

ASN

SER

4

ASP

PRO

MET

GLY

LYS

GLU

GLY

ASP

PHE

VAL

5

TYR

LYS

GLU

VAL

ILE

LYS

SER

PRO

THR

ALA

6

SER

ARG

ILE

SER

LEU

GLY

LYS

VAL

LYS

7

SER

VAL

LYS

GLU

THR

MET

ARG

LYS

ARG

MET

8

SER

LYS

TYR

SER

VAL

SER

GLU

9

GLN

ASP

SER

GLY

LEU

ASP

GLY

MET

PRO

GLY

10

SER

PRO

SER

GLN

PRO

ASP

PRO

GLU

11

HIS

LEU

ASP

LYS

PRO

LYS

LEU

LYS

ALA

GLY

12

GLY

SER

VAL

GLU

SER

LEU

ARG

SER

LEU

13

SER

GLY

GLN

ASN

SER

MET

SER

GLY

GLN

THR

14

VAL

SER

THR

ASP

SER

THR

SER

ASN

15

ARG

GLU

SER

VAL

LYS

SER

GLU

ASP

GLY

ASP

16

ASP

GLU

PRO

TYR

ARG

GLY

PRO

PHE

17

CYS

GLY

ARG

ALA

ARG

VAL

HIS

THR

ASP

Samples:

sample_1: SPIDER-SASH1, [U-100% 13C; U-100% 15N; U-80% 2H], 802 uM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D TROSY HNCACB	sample_1	isotropic	sample_conditions_1
3D TROSY HNCACO	sample_1	isotropic	sample_conditions_1
3D TROSY HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D TROSY HNCO	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5.1 - chemical shift assignment, data analysis

TOPSPIN v4.1.4 - collection, data analysis

NMRFAM-SPARKY v1.470 - data analysis

NMRPipe - data analysis, processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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