BMRB Entry 36244

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PDB ID:
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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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: Tsuda, K.; Kukimoto-Niino, M.; Ihara, K.; Mishima-Tsumagari, C.; Tomabechi, Y.; Yonemochi, M.; Inoue, M.; Hanada, H.; Shirouzu, M.. "Solution structure of the Rho GTPase binding domain (RBD) of ELMO1"  .

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:
Data typeCount
13C chemical shifts494
15N chemical shifts116
1H chemical shifts750

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 114 residues - 12765.462 Da.

1   GLYMETPROPROPROALAASPILEVALLYS
2   VALALAILEGLUTRPPROGLYALATYRPRO
3   LYSLEUMETGLUILEASPGLNLYSLYSPRO
4   LEUSERALAILEILELYSGLUVALCYSASP
5   GLYTRPSERLEUALAASNHISGLUTYRPHE
6   ALALEUGLNHISALAASPSERSERASNPHE
7   TYRILETHRGLULYSASNARGASNGLUILE
8   LYSASNGLYTHRILELEUARGLEUTHRTHR
9   SERPROALAGLNASNALAGLNGLNLEUHIS
10   GLUARGILEGLNSERSERSERMETASPALA
11   LYSLEUGLUALALEULYSASPLEUALASER
12   LEUSERARGASP

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:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_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