BMRB Entry 36244

Name: Solution structure of the Rho GTPase binding domain (RBD) of ELMO1
Published: 2023-02-23

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PDB ID: 6jpp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36244
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 Rho GTPase binding domain (RBD) of ELMO1

Deposition date:

2019-03-27

Original release date:

2023-02-23

Authors:

Tsuda, K.; Kukimoto-Niino, M.; Shirouzu, M.

Citation:

Citation: Tam, Chunlai; Kukimoto-Niino, Mutsuko; Miyata-Yabuki, Yukako; Tsuda, Kengo; Mishima-Tsumagari, Chiemi; Ihara, Kentaro; Inoue, Mio; Yonemochi, Mayumi; Hanada, Kazuharu; Matsumoto, Takehisa; Shirouzu, Mikako; Zhang, Kam. "Targeting Ras-binding domain of ELMO1 by computational nanobody design" Commun. Biol. 6, 284-284 (2023).
PubMed: 36932164

Assembly members:

Assembly members:
Engulfment and cell motility protein 1, polymer, 114 residues, 12765.462 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 BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Engulfment and cell motility protein 1: GMPPPADIVKVAIEWPGAYP KLMEIDQKKPLSAIIKEVCD GWSLANHEYFALQHADSSNF YITEKNRNEIKNGTILRLTT SPAQNAQQLHERIQSSSMDA KLEALKDLASLSRD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	494
15N chemical shifts	116
1H chemical shifts	750

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 114 residues - 12765.462 Da.

1

GLY

MET

PRO

ALA

ASP

ILE

VAL

LYS

2

VAL

ALA

ILE

GLU

TRP

PRO

GLY

ALA

TYR

PRO

3

LYS

LEU

MET

GLU

ILE

ASP

GLN

LYS

PRO

4

LEU

SER

ALA

ILE

LYS

GLU

VAL

CYS

ASP

5

GLY

TRP

SER

LEU

ALA

ASN

HIS

GLU

TYR

PHE

6

ALA

LEU

GLN

HIS

ALA

ASP

SER

ASN

PHE

7

TYR

ILE

THR

GLU

LYS

ASN

ARG

ASN

GLU

ILE

8

LYS

ASN

GLY

THR

ILE

LEU

ARG

LEU

THR

9

SER

PRO

ALA

GLN

ASN

ALA

GLN

LEU

HIS

10

GLU

ARG

ILE

GLN

SER

MET

ASP

ALA

11

LYS

LEU

GLU

ALA

LEU

LYS

ASP

LEU

ALA

SER

12

LEU

SER

ARG

ASP

Samples:

sample_1: Elmo1 RBD, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-2H], 10%

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

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Kujira, Kobayashi, N - data analysis

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 900 MHz

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