BMRB Entry 25730

Name: 1H, 15N and 13C backbone assignments of GDP-bound human H-Ras mutant G12V
Published: 2015-08-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25730

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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, 15N and 13C backbone assignments of GDP-bound human H-Ras mutant G12V

Deposition date:

2015-07-28

Original release date:

2015-08-27

Authors:

Amin, Nader; Chiarparin, Elisabetta; Coyle, Joe; Nietlispach, Daniel; Williams, Glyn

Citation:

Citation: Amin, Nader; Chiarparin, Elisabetta; Coyle, Joe; Nietlispach, Daniel; Williams, Glyn. "1H, 15N and 13C backbone assignments of GDP-bound human H-Ras mutant G12V" Biomol. NMR Assign. 10, 121-123.
PubMed: 26373425

Assembly members:

Assembly members:
H-Ras_G12V, polymer, 169 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: pET23b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H-Ras_G12V: GSHMTEYKLVVVGAVGVGKS ALTIQLIQNHFVDEYDPTIE DSYRKQVVIDGETCLLDILD TAGQEEYSAMRDQYMRTGEG FLCVFAINNTKSFEDIHQYR EQIKRVKDSDDVPMVLVGNK CDLAARTVESRQAQDLARSY GIPYIETSAKTRQGVEDAFY TLVREIRQH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	482
15N chemical shifts	160
1H chemical shifts	160

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H-Ras g12V	1

Entities:

Entity 1, H-Ras g12V 169 residues - Formula weight is not available

1

GLY

SER

HIS

MET

THR

GLU

TYR

LYS

LEU

VAL

2

VAL

GLY

ALA

VAL

GLY

VAL

GLY

LYS

SER

3

ALA

LEU

THR

ILE

GLN

LEU

ILE

GLN

ASN

HIS

4

PHE

VAL

ASP

GLU

TYR

ASP

PRO

THR

ILE

GLU

5

ASP

SER

TYR

ARG

LYS

GLN

VAL

ILE

ASP

6

GLY

GLU

THR

CYS

LEU

ASP

ILE

LEU

ASP

7

THR

ALA

GLY

GLN

GLU

TYR

SER

ALA

MET

8

ARG

ASP

GLN

TYR

MET

ARG

THR

GLY

GLU

GLY

9

PHE

LEU

CYS

VAL

PHE

ALA

ILE

ASN

THR

10

LYS

SER

PHE

GLU

ASP

ILE

HIS

GLN

TYR

ARG

11

GLU

GLN

ILE

LYS

ARG

VAL

LYS

ASP

SER

ASP

12

ASP

VAL

PRO

MET

VAL

LEU

VAL

GLY

ASN

LYS

13

CYS

ASP

LEU

ALA

ARG

THR

VAL

GLU

SER

14

ARG

GLN

ALA

GLN

ASP

LEU

ALA

ARG

SER

TYR

15

GLY

ILE

PRO

TYR

ILE

GLU

THR

SER

ALA

LYS

16

THR

ARG

GLN

GLY

VAL

GLU

ASP

ALA

PHE

TYR

17

THR

LEU

VAL

ARG

GLU

ILE

ARG

GLN

HIS

Samples:

sample_1: H-Ras G12V, [U-99% 13C; U-99% 15N], 300 mM; NaCl 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 500 MHz
Bruker DRX 600 MHz

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