BMRB Entry 36166

Name: Solution structure of H-RasT35S mutant protein in complex with KBFM123
Published: 2018-12-07

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PDB ID: 5zc6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36166
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of H-RasT35S mutant protein in complex with KBFM123

Deposition date:

2018-02-15

Original release date:

2018-12-07

Authors:

Matsumoto, S.; Hayashi, Y.; Hiraga, T.; Matsuo, K.; Kataoka, T.

Citation:

Citation: Matsumoto, S.; Hiraga, T.; Hayashi, Y.; Yoshikawa, Y.; Tsuda, C.; Araki, M.; Neya, M.; Shima, F.; Kataoka, T.. "Molecular Basis for Allosteric Inhibition of GTP-Bound H-Ras Protein by a Small-Molecule Compound Carrying a Naphthalene Ring" Biochemistry 57, .-. (2018).
PubMed: 30141910

Assembly members:

Assembly members:
GTPase HRas, polymer, 166 residues, 18861.166 Da.
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, non-polymer, 522.196 Da.
3-oxidanyl-~{N}-[[(2~{S})-oxolan-2-yl]methyl]naphthalene-2-carboxamide, non-polymer, 271.311 Da.
MAGNESIUM ION, non-polymer, 24.305 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GTPase HRas: MTEYKLVVVGAGGVGKSALT IQLIQNHFVDEYDPSIEDSY RKQVVIDGETCLLDILDTAG QEEYSAMRDQYMRTGEGFLC VFAINNTKSFEDIHQYREQI KRVKDSDDVPMVLVGNKCDL AARTVESRQAQDLARSYGIP YIETSAKTRQGVEDAFYTLV REIRQH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	5
1H chemical shifts	23

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_GNP	2
3	entity_KBF	3
4	entity_MG	4

Entities:

Entity 1, entity_1 166 residues - 18861.166 Da.

1

MET

THR

GLU

TYR

LYS

LEU

VAL

GLY

2

ALA

GLY

VAL

GLY

LYS

SER

ALA

LEU

THR

3

ILE

GLN

LEU

ILE

GLN

ASN

HIS

PHE

VAL

ASP

4

GLU

TYR

ASP

PRO

SER

ILE

GLU

ASP

SER

TYR

5

ARG

LYS

GLN

VAL

ILE

ASP

GLY

GLU

THR

6

CYS

LEU

ASP

ILE

LEU

ASP

THR

ALA

GLY

7

GLN

GLU

TYR

SER

ALA

MET

ARG

ASP

GLN

8

TYR

MET

ARG

THR

GLY

GLU

GLY

PHE

LEU

CYS

9

VAL

PHE

ALA

ILE

ASN

THR

LYS

SER

PHE

10

GLU

ASP

ILE

HIS

GLN

TYR

ARG

GLU

GLN

ILE

11

LYS

ARG

VAL

LYS

ASP

SER

ASP

VAL

PRO

12

MET

VAL

LEU

VAL

GLY

ASN

LYS

CYS

ASP

LEU

13

ALA

ARG

THR

VAL

GLU

SER

ARG

GLN

ALA

14

GLN

ASP

LEU

ALA

ARG

SER

TYR

GLY

ILE

PRO

15

TYR

ILE

GLU

THR

SER

ALA

LYS

THR

ARG

GLN

16

GLY

VAL

GLU

ASP

ALA

PHE

TYR

THR

LEU

VAL

17

ARG

GLU

ILE

ARG

GLN

HIS

Entity 2, entity_GNP - C10 H17 N6 O13 P3 - 522.196 Da.

1

GNP

Entity 3, entity_KBF - C16 H17 N O3 - 271.311 Da.

1

KBF

Entity 4, entity_MG - Mg - 24.305 Da.

1

MG

Samples:

sample_1: H-RasT35S, [U-99% 13C; U-99% 15N], 0.8 mM; KBFM123 3.0 mM; MAGNESIUM ION 8 mM; PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER 0.8 mM; sodium chloride 40 mM; sodium phosphate 20 mM; D2O, [U-2H], 80%; d6-DMSO, [U-2H], 20%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CNS, BRUNGER A. T. ET.AL. - refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz