BMRB Entry 51806

Name: 1H and 15N chemical shifts of RhoA mutant A161V bound to GDP
Published: 2024-06-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51806

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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:

1H and 15N chemical shifts of RhoA mutant A161V bound to GDP

Deposition date:

2023-01-25

Original release date:

2024-06-24

Authors:

Lin, Yuan; Ramelot, Theresa; Zheng, Yi

Citation:

Citation: Lin, Yuan; Ramelot, Theresa; Senyuz, Simge; Gursoy, Attila; Jang, Hyunbum; Nussinov, Ruth; Keskin, Ozlem; Zheng, Yi. "Tumor-derived RHOA mutants interact with effectors in the GDP-bound state" Nat. Commun. 15, 7176-7176 (2024).
PubMed: 39169042

Assembly members:

Assembly members:
entity_1, polymer, 181 residues, Formula weight is not available
entity_GDP, non-polymer, 443.201 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 Vector: pGEX-4T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAIRKKLVIVGDGACGKTC LLIVNSKDQFPEVYVPTVFE NYVADIEVDGKQVELALWDT AGQEDYDRLRPLSYPDTDVI LMCFSIDSPDSLENIPEKWT PEVKHFCPNVPIILVGNKKD LRNDEHTRRELAKMKQEPVK PEEGRDMANRIGAFGYMECS VKTKDGVREVFEMATRAALQ A

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	94
1H chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RhoA	1
2	GDP	2

Entities:

Entity 1, RhoA 181 residues - Formula weight is not available

RhoA 1-181 (full length 1-193, truncated at 182), contains F25N mutation for better protein expression. non-native GS at N-terminus.

1

MET

ALA

ILE

ARG

LYS

LEU

VAL

ILE

2

VAL

GLY

ASP

GLY

ALA

CYS

GLY

LYS

THR

CYS

3

LEU

ILE

VAL

ASN

SER

LYS

ASP

GLN

PHE

4

PRO

GLU

VAL

TYR

VAL

PRO

THR

VAL

PHE

GLU

5

ASN

TYR

VAL

ALA

ASP

ILE

GLU

VAL

ASP

GLY

6

LYS

GLN

VAL

GLU

LEU

ALA

LEU

TRP

ASP

THR

7

ALA

GLY

GLN

GLU

ASP

TYR

ASP

ARG

LEU

ARG

8

PRO

LEU

SER

TYR

PRO

ASP

THR

ASP

VAL

ILE

9

LEU

MET

CYS

PHE

SER

ILE

ASP

SER

PRO

ASP

10

SER

LEU

GLU

ASN

ILE

PRO

GLU

LYS

TRP

THR

11

PRO

GLU

VAL

LYS

HIS

PHE

CYS

PRO

ASN

VAL

12

PRO

ILE

LEU

VAL

GLY

ASN

LYS

ASP

13

LEU

ARG

ASN

ASP

GLU

HIS

THR

ARG

GLU

14

LEU

ALA

LYS

MET

LYS

GLN

GLU

PRO

VAL

LYS

15

PRO

GLU

GLY

ARG

ASP

MET

ALA

ASN

ARG

16

ILE

GLY

ALA

PHE

GLY

TYR

MET

GLU

CYS

SER

17

VAL

LYS

THR

LYS

ASP

GLY

VAL

ARG

GLU

VAL

18

PHE

GLU

MET

ALA

THR

ARG

ALA

LEU

GLN

19

ALA

Entity 2, GDP - C10 H15 N5 O11 P2 - 443.201 Da.

1

GDP

Samples:

sample_1: RhoA-A161V, [U-99% 15N], 0.8 ± 0.05 mM; TRIS 20 mM; sodium chloride 100 mM; magnesium chloride 5 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRFAM-SPARKY vv.1.370 powered by Sparky 3.19 - peak picking

NMRPipe vv10.9 - processing

TOPSPIN v3.6.0 - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz