BMRB Entry 36445

Name: Solution structure of the chimeric peptide of the first SURP domain of Human SF3A1 and the interacting region of SF1.
Published: 2022-10-03

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PDB ID: 7vh9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36445
MolProbity Validation Chart

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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: Solution structure of the chimeric peptide of the first SURP domain of Human SF3A1 and the interacting region of SF1. PubMed: 36173164

Deposition date: 2021-09-21 Original release date: 2022-10-03

Authors: Muto, Y.; Kuwasako, K.; Takizawa, M.; Kobayashi, N.; Sakamoto, T.

Citation: Nameki, Nobukazu; Takizawa, Masayuki; Suzuki, Takayuki; Tani, Shoko; Kobayashi, Naohiro; Sakamoto, Taiichi; Muto, Yutaka; Kuwasako, Kanako. "Structural basis for the interaction between the first SURP domain of the SF3A1 subunit in U2 snRNP and the human splicing factor SF1" Protein Sci. 31, e4437-e4437 (2022).

Assembly members:
entity_1, polymer, 111 residues, 12133.198 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET-15b

Entity Sequences (FASTA):
entity_1: GEVRNIVDKTASFVARNGPE FEARIRQNEINNPKFNFLNP NDPYHAYYRHKVSEFKEGKA QEPSSGSSGSSGSSGSSGQR PGDPQSAQDKARMDKEYLSL MAELGEAPVPA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	416
15N chemical shifts	98
1H chemical shifts	676

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 111 residues - 12133.198 Da.

1

GLY

GLU

VAL

ARG

ASN

ILE

VAL

ASP

LYS

THR

2

ALA

SER

PHE

VAL

ALA

ARG

ASN

GLY

PRO

GLU

3

PHE

GLU

ALA

ARG

ILE

ARG

GLN

ASN

GLU

ILE

4

ASN

PRO

LYS

PHE

ASN

PHE

LEU

ASN

PRO

5

ASN

ASP

PRO

TYR

HIS

ALA

TYR

ARG

HIS

6

LYS

VAL

SER

GLU

PHE

LYS

GLU

GLY

LYS

ALA

7

GLN

GLU

PRO

SER

GLY

SER

GLY

SER

8

SER

GLY

SER

GLY

SER

GLY

GLN

ARG

9

PRO

GLY

ASP

PRO

GLN

SER

ALA

GLN

ASP

LYS

10

ALA

ARG

MET

ASP

LYS

GLU

TYR

LEU

SER

LEU

11

MET

ALA

GLU

LEU

GLY

GLU

ALA

PRO

VAL

PRO

12

ALA

Samples:

sample_1: protein, [U-99% 13C; U-99% 15N], 1.4 mM; Sodium Phosphate, [U=100% 2H], 20 mM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_13C,15N-SEPARATED_NOESY SPECTRA	sample_1	isotropic	sample_conditions_1

Software:

Amber v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

MagRO-NMRView, Kobayshi, N. - chemical shift assignment

NMRPipe v2007, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - peak picking

TALOS v2007, Cornilescu, Delaglio and Bax - geometry optimization

TopSpin v2.1, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE 600 MHz

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