BMRB Entry 18461

Name: Chemical shift assignments and backbone dynamics of H-Ras-GppNHp bound to Ras-binding domain of cRaf1.
Published: 2012-06-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18461

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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:

Chemical shift assignments and backbone dynamics of H-Ras-GppNHp bound to Ras-binding domain of cRaf1.

Deposition date:

2012-05-15

Original release date:

2012-06-26

Authors:

Araki, Mitsugu; Tamura, Atsuo

Citation:

Citation: Araki, Mitsugu; Shima, Fumi; Yoshikawa, Yoko; Muraoka, Shin; Ijiri, Yuichi; Nagahara, Yuka; Shirono, Tomoya; Kataoka, Tohru; Tamura, Atsuo. "Solution structure of the state 1 conformer of GTP-bound H-Ras protein and distinct dynamic properties between the state 1 and state 2 conformers" J. Biol. Chem. 286, 39644-39653 (2011).
PubMed: 21930707

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, 18861.303 Da.
entity_GNP, non-polymer, 522.196 Da.
entity_MG, non-polymer, 24.305 Da.
entity_HOH, water, 18.015 Da.
entry_2, polymer, . 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: pGEX-6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSDMTEYKLVVVGAGGV GKSALTIQLIQNHFVDEYDP TIEDSYRKQVVIDGETCLLD ILDTAGQEEYSAMRDQYMRT GEGFLCVFAINNTKSFEDIH QYREQIKRVKDSDDVPMVLV GNKCDLAARTVESRQAQDLA RSYGIPYIETSAKTRQGVED AFYTLVREIRQH
entry_2: XXXSNTIRVFLPNKQRTVVN VRNGMSLHDCLMKALKVRGL QPECCAVFRLLHEHKGKKAR LDWNTDAASLIGEELQVDF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1

Data type	Count
1H chemical shifts	162
13C chemical shifts	163
15N chemical shifts	162
heteronuclear NOE values	134
T1 relaxation values	134
T2 relaxation values	135

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H-Ras-GppNHp	1
2	PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER	2
3	MAGNESIUM ION	3
4	water	4
5	Ras-binding domain of cRaf1	5

Entities:

Entity 1, H-Ras-GppNHp 172 residues - 18861.303 Da.

1

GLY

PRO

LEU

GLY

SER

ASP

MET

THR

GLU

TYR

2

LYS

LEU

VAL

GLY

ALA

GLY

VAL

3

GLY

LYS

SER

ALA

LEU

THR

ILE

GLN

LEU

ILE

4

GLN

ASN

HIS

PHE

VAL

ASP

GLU

TYR

ASP

PRO

5

THR

ILE

GLU

ASP

SER

TYR

ARG

LYS

GLN

VAL

6

VAL

ILE

ASP

GLY

GLU

THR

CYS

LEU

ASP

7

ILE

LEU

ASP

THR

ALA

GLY

GLN

GLU

TYR

8

SER

ALA

MET

ARG

ASP

GLN

TYR

MET

ARG

THR

9

GLY

GLU

GLY

PHE

LEU

CYS

VAL

PHE

ALA

ILE

10

ASN

THR

LYS

SER

PHE

GLU

ASP

ILE

HIS

11

GLN

TYR

ARG

GLU

GLN

ILE

LYS

ARG

VAL

LYS

12

ASP

SER

ASP

VAL

PRO

MET

VAL

LEU

VAL

13

GLY

ASN

LYS

CYS

ASP

LEU

ALA

ARG

THR

14

VAL

GLU

SER

ARG

GLN

ALA

GLN

ASP

LEU

ALA

15

ARG

SER

TYR

GLY

ILE

PRO

TYR

ILE

GLU

THR

16

SER

ALA

LYS

THR

ARG

GLN

GLY

VAL

GLU

ASP

17

ALA

PHE

TYR

THR

LEU

VAL

ARG

GLU

ILE

ARG

18

GLN

HIS

Entity 2, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER - C10 H17 N6 O13 P3 - 522.196 Da.

1

GNP

Entity 3, MAGNESIUM ION - Mg - 24.305 Da.

1

MG

Entity 4, water - 18.015 Da.

1

HOH

Entity 5, Ras-binding domain of cRaf1 - Formula weight is not available

1

X

SER

ASN

THR

ILE

ARG

VAL

PHE

2

LEU

PRO

ASN

LYS

GLN

ARG

THR

VAL

ASN

3

VAL

ARG

ASN

GLY

MET

SER

LEU

HIS

ASP

CYS

4

LEU

MET

LYS

ALA

LEU

LYS

VAL

ARG

GLY

LEU

5

GLN

PRO

GLU

CYS

ALA

VAL

PHE

ARG

LEU

6

LEU

HIS

GLU

HIS

LYS

GLY

LYS

ALA

ARG

7

LEU

ASP

TRP

ASN

THR

ASP

ALA

SER

LEU

8

ILE

GLY

GLU

LEU

GLN

VAL

ASP

PHE

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

Related Database Links:

BMRB	10051 17183 17610 17678 18479 18629 25730
PDB	121P 1AA9 1AGP 1BKD 1CLU 1CRP 1CRQ 1CRR 1CTQ 1GNP 1GNQ 1GNR 1HE8 1IAQ 1IOZ 1JAH 1JAI 1K8R 1LF0 1LF5 1LFD 1NVU 1NVV 1NVW 1NVX 1P2S 1P2T 1P2U 1P2V 1PLJ 1PLK 1PLL 1Q21 1QRA 1RVD 1WQ1 1XCM 1XD2 1XJ0 1ZVQ 1ZW6 221P 2C5L 2CE2 2CL0 2CL6 2CL7 2CLC 2CLD 2EVW 2LCF 2LWI 2N42 2N46 2Q21 2QUZ 2RGA 2RGB 2RGC 2RGD 2RGE 2RGG 2UZI 2VH5 2X1V 3DDC 3I3S 3K8Y 3K9L 3K9N 3KKM 3KKN 3KUD 3L8Y 3L8Z 3LBH 3LBI 3LBN 3LO5 3OIU 3OIV 3OIW 3RRY 3RRZ 3RS0 3RS2 3RS3 3RS4 3RS5 3RS7 3RSL 3RSO 3TGP 3V4F 421P 4DLR 4DLS 4DLT 4DLU 4DLV 4DLW 4DLX 4DLY 4DLZ 4EFL 4EFM 4EFN 4G0N 4G3X 4K81 4L9S 4L9W 4NYI 4NYJ 4NYM 4Q21 4RSG 4URU 4URV 4URW 4URX 4URY 4URZ 4US0 4US1 4US2 4XVQ 4XVR 521P 5P21 621P 6Q21 721P 821P 1C1Y 1GUA 1RFA 1RRB 3KUC 3KUD 4G0N 4G3X
DBJ	BAB61869 BAB61870 BAB88314 BAB88315 BAB88316 BAB39743 BAB39748 BAB83675 BAE24820 BAG10817
EMBL	CAA25322 CAA25624 CAA27258 CAA35240 CAA90306 CAA27204 CAH92939
GB	AAA36554 AAA42009 AAA46568 AAA46569 AAA46570 AAA42001 AAB27591 AAH15273 AAH18119 AAH62071
PIR	A43816 TVMVNS
PRF	0904302A 1604384A
REF	NP_001017003 NP_001018465 NP_001084278 NP_001091711 NP_001123913 NP_001095975 NP_001126730 NP_001253231 NP_002871 NP_036771
SP	P01112 P01113 P01114 P01115 P08642 A7E3S4 P04049 P11345 Q5R5M7 Q99N57
TPG	DAA13500 DAA16778 DAA16781 DAA16798
AlphaFold	P01112 P01113 P01114 P01115 P08642 A7E3S4 P04049 P11345 Q5R5M7 Q99N57

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

BMRB Entry 18461

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: