BMRB Entry 51700

Name: Backbone chemical shifts of human SAFB2 SAP domain
Published: 2023-01-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51700

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 chemical shifts of human SAFB2 SAP domain

Deposition date:

2022-11-21

Original release date:

2023-01-30

Authors:

Korn, Sophie; Schlundt, Andreas

Citation:

Citation: Korn, Sophie; Von Ehr, Julian; Dhamotharan, Karthikeyan; Tants, Jan-Niklas; Abele, Rupert; Schlundt, Andreas. "Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein" Int. J. Mol. Sci. 24, 3286-3286 (2023).
PubMed: 36834708

Assembly members:

Assembly members:
entity_1, polymer, 53 residues, 5868.77 Da.

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: pETTrx1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGVAETGTRRLSELRVID LRAELKKRNLDTGGNKSVLM ERLKKAVKEEGQD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	152
15N chemical shifts	52
1H chemical shifts	180

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SAP_A, chain 1	1
2	SAP_A, chain 2	1

Entities:

Entity 1, SAP_A, chain 1 53 residues - 5868.77 Da.

Residues GAM (18-20) are artifacts from TEV cleavage, the natural sequence starts at Gly 21.

1

GLY

ALA

MET

GLY

VAL

ALA

GLU

THR

GLY

THR

2

ARG

LEU

SER

GLU

LEU

ARG

VAL

ILE

ASP

3

LEU

ARG

ALA

GLU

LEU

LYS

ARG

ASN

LEU

4

ASP

THR

GLY

ASN

LYS

SER

VAL

LEU

MET

5

GLU

ARG

LEU

LYS

ALA

VAL

LYS

GLU

6

GLY

GLN

ASP

Samples:

sample_1: SAP dimer, [U-99% 15N], 0.25 ± 0.05 mM; NaCl 250 ± 2.5 mM; Bis-Tris 20 ± 0.2 mM

sample_2: SAP dimer, [U-98% 13C; U-98% 15N], 1 ± 0.2 mM; NaCl 250 ± 2.5 mM; Bis-Tris 20 ± 0.2 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_1
3D HBHANH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v4 - collection, processing

ANALYSIS v2.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz
Bruker AVANCE NEO 600 MHz

UNP	Q14151
AlphaFold	Q8TB13