BMRB Entry 34643

Name: Solution structure of the human SF3A1 ubiquitin-like domain
Published: 2022-02-04

Click here to enlarge.

PDB ID: 7p08
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34643
MolProbity Validation Chart

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:

Solution structure of the human SF3A1 ubiquitin-like domain

Deposition date:

2021-06-29

Original release date:

2022-02-04

Authors:

de Vries, T.; Campagne, S.; Allain, F.

Citation:

Citation: de Vries, T.; Martelly, W.; Campagne, S.; Sabath, K.; Sarnowski, C.; Wong, J.; Leitner, A.; Jonas, S.; Sharma, S.; Allain, F.. "Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly" Proc. Natl. Acad. Sci. U. S. A. 119, e2114092119-e2114092119 (2022).
PubMed: 35101980

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 10238.928 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: pET24b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGSPVSIKVQVPNMQDKTEW KLNGQVLVFTLPLTDQVSVI KVKIHEATGMPAGKQKLQYE GIFIKDSNSLAYYNMANGAV IHLALKERGGRKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	409
15N chemical shifts	99
1H chemical shifts	684

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 93 residues - 10238.928 Da.

1

GLY

SER

PRO

VAL

SER

ILE

LYS

VAL

GLN

2

VAL

PRO

ASN

MET

GLN

ASP

LYS

THR

GLU

TRP

3

LYS

LEU

ASN

GLY

GLN

VAL

LEU

VAL

PHE

THR

4

LEU

PRO

LEU

THR

ASP

GLN

VAL

SER

VAL

ILE

5

LYS

VAL

LYS

ILE

HIS

GLU

ALA

THR

GLY

MET

6

PRO

ALA

GLY

LYS

GLN

LYS

LEU

GLN

TYR

GLU

7

GLY

ILE

PHE

ILE

LYS

ASP

SER

ASN

SER

LEU

8

ALA

TYR

ASN

MET

ALA

ASN

GLY

ALA

VAL

9

ILE

HIS

LEU

ALA

LEU

LYS

GLU

ARG

GLY

10

ARG

LYS

Samples:

sample_1: SF3A1, [U-13C; U-15N], 2.0 ± 0.1 mM; Sodium phosphate 10 mM; NaCl 50 mM

sample_2: SF3A1, [U-100% 15N], 1.1 ± 0.1 mM; Sodium phosphate 10 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 60 mM; pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 15N-1H HSQC NOESY	sample_1	isotropic	sample_conditions_1
3D 13Cali-1H HSQC NOESY	sample_1	isotropic	sample_conditions_1
3D 13Caro-1H HSQC NOESY	sample_1	isotropic	sample_conditions_1
{1H}-15N heteronuclear NOE	sample_2	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker AVANCE 900 MHz
Bruker AVIII 700 MHz
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