BMRB Entry 31193

Name: Structure of the C-terminal Domain of RAGE and Its Inhibitor
Published: 2025-08-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31193

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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:

Structure of the C-terminal Domain of RAGE and Its Inhibitor

Deposition date:

2024-08-09

Original release date:

2025-08-08

Authors:

Theophall, G.; Ramasamy, R.; Schmidt, A.; Manigrasso, M.; Shekthman, A.

Citation:

Citation: Theophall, G.; Ramasamy, R.; Schmidt, A.; Manigrasso, M.; Shekthman, A.. "Solution NMR Structure of ctRAGE bound to small molecule inhibitor" .

Assembly members:

Assembly members:
entity_1, polymer, 43 residues, 5017.203 Da.
entity_2, non-polymer, 412.484 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(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LWQRRQRRGEERKAPENQEE EEERAELNQSEEPEAGESST GGP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	112
15N chemical shifts	40
1H chemical shifts	230

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 43 residues - 5017.203 Da.

1

LEU

TRP

GLN

ARG

GLN

ARG

GLY

GLU

2

GLU

ARG

LYS

ALA

PRO

GLU

ASN

GLN

GLU

3

GLU

ARG

ALA

GLU

LEU

ASN

GLN

SER

4

GLU

PRO

GLU

ALA

GLY

GLU

SER

THR

5

GLY

PRO

Entity 2, unit_2 - C25 H24 N4 O2 - 412.484 Da.

1

A1A2E

Samples:

sample_1: ctRAGE, [U-13C; U-15N], 40 uM; RAGE406R 100 uM

sample_2: ctRAGE, [U-13C; U-15N], 40 uM

sample_conditions_1: ionic strength: 60 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA v20.12.24, Elmar Krieger, Kornel Ozvoldik, Dr. Henk-Jan Joosten, Gert Vriend - refinement

XEASY, Bartels et al. - peak picking

NMR spectrometers:

Bruker AVANCE 600 MHz

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