BMRB Entry 28064

Name: Solution structure of hSNF5 RPT1 domain
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28064

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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 hSNF5 RPT1 domain

Deposition date:

2020-01-22

Original release date:

2021-07-16

Authors:

Han, Jeongmin; Kim, Iktae; Suh, Jeong-Yong; Lee, Weontae

Citation:

Citation: Han, Jeongmin; Kim, Iktae; Park, Jae-Hyun; Yun, Ji-Hye; Joo, Keehyoung; Kim, Taehee; Park, Gye-Young; Ryu, Kyoung-Seok; Ko, Yoon-Joo; Mizutani, Kenji; Park, Sam-Young; Seong, Rho Hyun; Lee, Jooyoung; Suh, Jeong-Yong; Lee, Weontae. "A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction" Int. J. Mol. Sci. 21, 2452-2452 (2020).
PubMed: 32244797

Assembly members:

Assembly members:
RPT1, polymer, 88 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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RPT1: HDPAVIHENASQPEVLVPIR LDMEIDGQKLRDAFTWNMNE KLMTPEMFSEILCDDLDLNP LTFVPAIASAIRQQIESYPT DSILEDQS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	170
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1

Entities:

Entity 1, subunit 1 88 residues - Formula weight is not available

1

HIS

ASP

PRO

ALA

VAL

ILE

HIS

GLU

ASN

ALA

2

SER

GLN

PRO

GLU

VAL

LEU

VAL

PRO

ILE

ARG

3

LEU

ASP

MET

GLU

ILE

ASP

GLY

GLN

LYS

LEU

4

ARG

ASP

ALA

PHE

THR

TRP

ASN

MET

ASN

GLU

5

LYS

LEU

MET

THR

PRO

GLU

MET

PHE

SER

GLU

6

ILE

LEU

CYS

ASP

LEU

ASP

LEU

ASN

PRO

7

LEU

THR

PHE

VAL

PRO

ALA

ILE

ALA

SER

ALA

8

ILE

ARG

GLN

ILE

GLU

SER

TYR

PRO

THR

9

ASP

SER

ILE

LEU

GLU

ASP

GLN

SER

Samples:

sample_1: RPT1, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; HEPES 10 mM; sodium chloride 100 mM; DTT 2 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

SPARKY vNMRFAM-SPARKY, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, processing

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 850 MHz

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