BMRB Entry 51110

Name: Backbone 1H, 15N Chemical Shift Assignments for RGL1-Ras-association domain
Published: 2022-03-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51110

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 15N Chemical Shift Assignments for RGL1-Ras-association domain

Deposition date:

2021-09-29

Original release date:

2022-03-11

Authors:

Eves, Ben; Gebregiworgis, Teklab; Gasmi-Seabrook, Genevieve; Kuntz, Douglas; Prive, Gilbert; Marshall, Christopher; Ikura, Mitsu

Citation:

Citation: Eves, Ben; Gebregiworgis, Teklab; Gasmi-Seabrook, Genevieve; Kuntz, Douglas; Prive, Gilbert; Marshall, Christopher; Ikura, Mitsu. "Structures of RGL1 RAS-Association domain in complex with KRAS and the oncogenic G12V mutant" J. Mol. Biol. 434, 167527-167527 (2022).
PubMed: 35257782

Assembly members:

Assembly members:
entity_1, polymer, 93 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: pGEXascpac

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QQNEDTCIIRISVEDNNGNM YKSIMLTSQDKTPAVIQRAM LKHNLDSDPAEEYELVQVIS EDKELVIPDSANVFYAMNSQ VNFDFILRKKNSM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	76
1H chemical shifts	76

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RGL1-Ras-association domain monomer	1

Entities:

Entity 1, RGL1-Ras-association domain monomer 93 residues - Formula weight is not available

1

GLN

ASN

GLU

ASP

THR

CYS

ILE

ARG

2

ILE

SER

VAL

GLU

ASP

ASN

GLY

ASN

MET

3

TYR

LYS

SER

ILE

MET

LEU

THR

SER

GLN

ASP

4

LYS

THR

PRO

ALA

VAL

ILE

GLN

ARG

ALA

MET

5

LEU

LYS

HIS

ASN

LEU

ASP

SER

ASP

PRO

ALA

6

GLU

TYR

GLU

LEU

VAL

GLN

VAL

ILE

SER

7

GLU

ASP

LYS

GLU

LEU

VAL

ILE

PRO

ASP

SER

8

ALA

ASN

VAL

PHE

TYR

ALA

MET

ASN

SER

GLN

9

VAL

ASN

PHE

ASP

PHE

ILE

LEU

ARG

LYS

10

ASN

SER

MET

Samples:

sample_1: RGL1-Ras-association domain, [U-13C; U-15N], 200 uM; HEPES pH 7.4 20 mM; NaCl 100 mM; TCEP 2 mM; MgCl2 5 mM; sodium azide 0.01%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment, peak picking

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

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