BMRB Entry 15525

Name: 1H, 13C and 15N Resonance assignments for the human RLIP76 Ral binding domain and RalB in complex
Published: 2008-10-14

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15525

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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:

1H, 13C and 15N Resonance assignments for the human RLIP76 Ral binding domain and RalB in complex

Deposition date:

2007-10-15

Original release date:

2008-10-14

Authors:

Fenwick, Robert; Prasannan, Sunil; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen

Citation:

Citation: Fenwick, R Bryn; Prasannan, Sunil; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "Resonance assignments for the RLIP76 Ral binding domain in its free form and in complex with the small G protein RalB" Biomol. NMR Assignments 2, 191-194 (2008).
PubMed: 19636902

Assembly members:

Assembly members:
RLIP76, polymer, 56 residues, Formula weight is not available
RalB, polymer, 188 residues, Formula weight is not available
GNP, non-polymer, 522.196 Da.
MG, non-polymer, 24.305 Da.
HOH, non-polymer, 18.015 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-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RLIP76: GSETQAGIKEEIRRQEFLLN SLHRDLQGGIKDLSKEERLW EVQRILTALKRKLREA
RalB: GSHMAANKSKGQSSLALHKV IMVGSGGVGKSALTLQFMYD EFVEDYEPTKADSYRKKVVL DGEEVQIDILDTAGLEDYAA IRDNYFRSGEGFLLVFSITE HESFTATAEFREQILRVKAE EDKIPLLVVGNKSDLEERRQ VPVEEARSKAEEWGVQYVET SAKTRANVDKVFFDLMREIR TKKMSENK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	1007
15N chemical shifts	250
1H chemical shifts	1707

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RLIP76	1
2	RalB	2
3	GMPPNP	3
4	Magnesium ion	4
5	BOUND WATER, 1	5
6	BOUND WATER, 2	5

Entities:

Entity 1, RLIP76 56 residues - Formula weight is not available

The first two residues are a tag remnant. The protein starts at E393 and ends at A446

1

GLY

SER

GLU

THR

GLN

ALA

GLY

ILE

LYS

GLU

2

GLU

ILE

ARG

GLN

GLU

PHE

LEU

ASN

3

SER

LEU

HIS

ARG

ASP

LEU

GLN

GLY

ILE

4

LYS

ASP

LEU

SER

LYS

GLU

ARG

LEU

TRP

5

GLU

VAL

GLN

ARG

ILE

LEU

THR

ALA

LEU

LYS

6

ARG

LYS

LEU

ARG

GLU

ALA

Entity 2, RalB 188 residues - Formula weight is not available

The first three residues are a tag remnant. The protein starts at M1 and ends at K185

1

GLY

SER

HIS

MET

ALA

ASN

LYS

SER

LYS

2

GLY

GLN

SER

LEU

ALA

LEU

HIS

LYS

VAL

3

ILE

MET

VAL

GLY

SER

GLY

VAL

GLY

LYS

4

SER

ALA

LEU

THR

LEU

GLN

PHE

MET

TYR

ASP

5

GLU

PHE

VAL

GLU

ASP

TYR

GLU

PRO

THR

LYS

6

ALA

ASP

SER

TYR

ARG

LYS

VAL

LEU

7

ASP

GLY

GLU

VAL

GLN

ILE

ASP

ILE

LEU

8

ASP

THR

ALA

GLY

LEU

GLU

ASP

TYR

ALA

9

ILE

ARG

ASP

ASN

TYR

PHE

ARG

SER

GLY

GLU

10

GLY

PHE

LEU

VAL

PHE

SER

ILE

THR

GLU

11

HIS

GLU

SER

PHE

THR

ALA

THR

ALA

GLU

PHE

12

ARG

GLU

GLN

ILE

LEU

ARG

VAL

LYS

ALA

GLU

13

GLU

ASP

LYS

ILE

PRO

LEU

VAL

GLY

14

ASN

LYS

SER

ASP

LEU

GLU

ARG

GLN

15

VAL

PRO

VAL

GLU

ALA

ARG

SER

LYS

ALA

16

GLU

TRP

GLY

VAL

GLN

TYR

VAL

GLU

THR

17

SER

ALA

LYS

THR

ARG

ALA

ASN

VAL

ASP

LYS

18

VAL

PHE

ASP

LEU

MET

ARG

GLU

ILE

ARG

19

THR

LYS

MET

SER

GLU

ASN

LYS

Entity 3, GMPPNP - C10 H17 N6 O13 P3 - 522.196 Da.

1

GNP

Entity 4, Magnesium ion - Mg - 24.305 Da.

1

MG

Entity 5, BOUND WATER, 1 - H2 O - 18.015 Da.

1

HOH

Samples:

15N_RLIP76: RLIP76, [U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RalB 0.66 mM; magnesium chloride 1 mM

13C_15N_RLIP76: RLIP76, [U-98% 13C; U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RalB 0.66 mM; magnesium chloride 1 mM

15N_RalB: RalB, [U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RLIP76 0.66 mM; magnesium chloride 1 mM

13C_15N_RalB: RalB, [U-98% 13C; U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RLIP76 0.66 mM; magnesium chloride 1 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	13C_15N_RLIP76	isotropic	sample_conditions_1
3D HNCA	13C_15N_RLIP76	isotropic	sample_conditions_1
3D HNCO	13C_15N_RLIP76	isotropic	sample_conditions_1
3D HN(CO)CA	13C_15N_RLIP76	isotropic	sample_conditions_1
3D HNCACB	13C_15N_RLIP76	isotropic	sample_conditions_1
3D (H)C(CCO)NH	13C_15N_RLIP76	isotropic	sample_conditions_1
3D HBHA(CO)NH	13C_15N_RLIP76	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C_15N_RLIP76	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_RLIP76	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C_15N_RLIP76	isotropic	sample_conditions_1
2D 1H-13C HSQC	13C_15N_RLIP76	isotropic	sample_conditions_1
2D 1H-15N HSQC	13C_15N_RalB	isotropic	sample_conditions_2
3D HNCA	13C_15N_RalB	isotropic	sample_conditions_2
3D HNCO	13C_15N_RalB	isotropic	sample_conditions_2
3D HN(CO)CA	13C_15N_RalB	isotropic	sample_conditions_2
3D HNCACB	13C_15N_RalB	isotropic	sample_conditions_2
3D (H)C(CCO)NH	13C_15N_RalB	isotropic	sample_conditions_2
3D CBCA(CO)NH	13C_15N_RalB	isotropic	sample_conditions_2
3D HCCH-TOCSY	13C_15N_RalB	isotropic	sample_conditions_2
3D 1H-15N NOESY	15N_RalB	isotropic	sample_conditions_2
3D 1H-13C NOESY	13C_15N_RalB	isotropic	sample_conditions_2
2D 1H-13C HSQC	13C_15N_RalB	isotropic	sample_conditions_2

Software:

AZARA, Boucher - processing

Analysis, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides and Laue - chemical shift assignment

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 500 MHz
Bruker DRX 600 MHz
Bruker DRX 800 MHz

BMRB	15524 15230 15803
PDB	2KWH 2KWI 2KE5 2KWI
GB	AAI45321 AAA60250 AAH18163 AAI46174 AAM12625 AAP35599
REF	XP_004656898 NP_001091454 NP_001126995 NP_001244728 NP_002872 XP_001492315
DBJ	BAE02438 BAG35360 BAG64302 BAJ20798
EMBL	CAA33119 CAH93398
SP	P11234 Q4R379 Q5R4B8
TPG	DAA32595
AlphaFold	Q5R4B8 P11234 Q4R379