BMRB Entry 51701

Name: Backbone chemical shifts of human SAFB2 RRM domain at pH 5.0
Published: 2023-01-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51701

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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 chemical shifts of human SAFB2 RRM domain at pH 5.0

Deposition date:

2022-11-21

Original release date:

2023-01-30

Authors:

Schlundt, Andreas; Korn, Sophie

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, 85 residues, 9131.46 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: GAMGSGRNLWVSGLSSTTRA TDLKNLFSKYGKVVGAKVVT NARSPGARCYGFVTMSTSDE ATKCISHLHRTELHGRMISV EKAKN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	246
15N chemical shifts	84
1H chemical shifts	87

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SAFB2 RRM domain	1

Entities:

Entity 1, SAFB2 RRM domain 85 residues - 9131.46 Da.

Residues GAM (401-403) are artifacts from TEV cleavage, the natural sequence starts at Gly 404.

1

GLY

ALA

MET

GLY

SER

GLY

ARG

ASN

LEU

TRP

2

VAL

SER

GLY

LEU

SER

THR

ARG

ALA

3

THR

ASP

LEU

LYS

ASN

LEU

PHE

SER

LYS

TYR

4

GLY

LYS

VAL

GLY

ALA

LYS

VAL

THR

5

ASN

ALA

ARG

SER

PRO

GLY

ALA

ARG

CYS

TYR

6

GLY

PHE

VAL

THR

MET

SER

THR

SER

ASP

GLU

7

ALA

THR

LYS

CYS

ILE

SER

HIS

LEU

HIS

ARG

8

THR

GLU

LEU

HIS

GLY

ARG

MET

ILE

SER

VAL

9

GLU

LYS

ALA

LYS

ASN

Samples:

sample_1: SAFB2 RRM domain, [U-99% 15N], 620 ± 12.4 uM; NaCl 150 ± 1.5 mM; Bis-Tris 20 ± 0.2 mM; TCEP 2 ± 0.02 mM

sample_2: SAFB2 RRM domain, [U-98% 13C; U-98% 15N], 440 ± 8.8 uM; NaCl 150 ± 1.5 mM; Bis-Tris 20 ± 0.2 mM; TCEP 2 ± 0.02 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.0; 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 HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4 - collection, processing

ANALYSIS v2.3 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz
Bruker AVANCE NEO 900 MHz

UNP	Q14151
AlphaFold	Q8TB13