BMRB Entry 52393

Name: StREM13 150-198
Published: 2024-09-05

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PDB ID: 9f1g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52393
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:

StREM13 150-198

Deposition date:

2024-04-09

Original release date:

2024-09-05

Authors:

XU, Zeren; Habenstein, Birgit; Legrand, Anthony; Berbon, Melanie; Grelard, Axelle; Morvan, Estelle; Loquet, Antoine

Citation:

Citation: XU, Zeren; Habenstein, Birgit; Legrand, Anthony; Berbon, Melanie; Grelard, Axelle; Morvan, Estelle; Loquet, Antoine. "Dynamic pre-structuration of lipid nanodomain-segregating remorin proteins" .

Assembly members:

Assembly members:
entity_1, polymer, 49 residues, 5465.452 Da.

Natural source:

Natural source: Common Name: potato Taxonomy ID: 4113 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Solanum tuberosum

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NKIALLHKEAEEKRAMIEAK RGEDLLKAEELAAKYRATGT APKKILGIF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	49
1H chemical shifts	346

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	REM-CA	1

Entities:

Entity 1, REM-CA 49 residues - 5465.452 Da.

1

ASN

LYS

ILE

ALA

LEU

HIS

LYS

GLU

ALA

2

GLU

LYS

ARG

ALA

MET

ILE

GLU

ALA

LYS

3

ARG

GLY

GLU

ASP

LEU

LYS

ALA

GLU

4

LEU

ALA

LYS

TYR

ARG

ALA

THR

GLY

THR

5

ALA

PRO

LYS

ILE

LEU

GLY

ILE

PHE

Samples:

sample_1: StREM1.3/150-198 1 mM

sample_conditions_4: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_4
2D 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_4
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_4

Software:

CcpNMR vV2 - chemical shift assignment, data analysis, peak picking

TOPSPIN v4.1.2 - collection, processing

NMR spectrometers:

Bruker Biospin AVANCE NEO 18,79T (800MHz) MHz

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