BMRB Entry 15230

Name: 1H, 13C and 15N resonance assignments for the small GTPase RalB in its active conformation
Published: 2007-08-22

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15230

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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, 13C and 15N resonance assignments for the small GTPase RalB in its active conformation

Deposition date:

2007-04-30

Original release date:

2007-08-22

Authors:

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

Citation:

Citation: Prasannan, Sunil; Fenwick, R. Bryn; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation" Biomol. NMR Assignments 1, 147-149 (2007).
PubMed: 19636851

Assembly members:

Assembly members:
RalB, polymer, 186 residues, Formula weight is not available
GNP, non-polymer, Formula weight is not available
MG, non-polymer, Formula weight is not available
WATER, water, 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: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RalB: HMAANKSKGQSSLALHKVIM VGSGGVGKSALTLQFMYDEF VEDYEPTKADSYRKKVVLDG EEVQIDILDTAGLEDYAAIR DNYFRSGEGFLLVFSITEHE SFTATAEFREQILRVKAEED KIPLLVVGNKSDLEERRQVP VEEARSKAEEWGVQYVETSA KTRANVDKVFFDLMREIRTK KMSENK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
order_parameters
- order_parameter_list_1

Data type	Count
13C chemical shifts	776
15N chemical shifts	178
1H chemical shifts	1243
T1 relaxation values	127
T2 relaxation values	127
heteronuclear NOE values	127
order parameters	127

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RalB	1
2	GMPPNP	2
3	MAGNESIUM ION	3
4	BOUND WATER, 1	4
5	BOUND WATER, 2	4

Entities:

Entity 1, RalB 186 residues - Formula weight is not available

Residues 0 (H) from His-Tag. Residues Met1 to Ser11 not assigned, due to proteolysis

1

HIS

MET

ALA

ASN

LYS

SER

LYS

GLY

GLN

2

SER

LEU

ALA

LEU

HIS

LYS

VAL

ILE

MET

3

VAL

GLY

SER

GLY

VAL

GLY

LYS

SER

ALA

4

LEU

THR

LEU

GLN

PHE

MET

TYR

ASP

GLU

PHE

5

VAL

GLU

ASP

TYR

GLU

PRO

THR

LYS

ALA

ASP

6

SER

TYR

ARG

LYS

VAL

LEU

ASP

GLY

7

GLU

VAL

GLN

ILE

ASP

ILE

LEU

ASP

THR

8

ALA

GLY

LEU

GLU

ASP

TYR

ALA

ILE

ARG

9

ASP

ASN

TYR

PHE

ARG

SER

GLY

GLU

GLY

PHE

10

LEU

VAL

PHE

SER

ILE

THR

GLU

HIS

GLU

11

SER

PHE

THR

ALA

THR

ALA

GLU

PHE

ARG

GLU

12

GLN

ILE

LEU

ARG

VAL

LYS

ALA

GLU

ASP

13

LYS

ILE

PRO

LEU

VAL

GLY

ASN

LYS

14

SER

ASP

LEU

GLU

ARG

GLN

VAL

PRO

15

VAL

GLU

ALA

ARG

SER

LYS

ALA

GLU

16

TRP

GLY

VAL

GLN

TYR

VAL

GLU

THR

SER

ALA

17

LYS

THR

ARG

ALA

ASN

VAL

ASP

LYS

VAL

PHE

18

PHE

ASP

LEU

MET

ARG

GLU

ILE

ARG

THR

LYS

19

LYS

MET

SER

GLU

ASN

LYS

Entity 2, GMPPNP - Formula weight is not available

1

GNP

Entity 3, MAGNESIUM ION - Formula weight is not available

1

MG

Entity 4, BOUND WATER, 1 - 18.015 Da.

1

HOH

Samples:

sample_1: RalB, [U-99% 13C; U-99% 15N], 0.6 mM; GMPPNP, none, 0.6 mM; Magnesium chloride, none, 1 mM; sodium chloride, none, 100 mM; D2O, none, 10%; sodium azide, none, 0.05%; sodium phosphate, none, 50 mM

sample_2: RalB, [U-99% 15N], 0.6 mM; GMPPNP, none, 0.6 mM; Magnesium chloride, none, 1 mM; sodium chloride, none, 100 mM; D2O, none, 10%; sodium azide, none, 0.05%; sodium phosphate, none, 50 mM

sample_3: RalB, none, 0.6 mM; GMPPNP, none, 0.6 mM; Magnesium chloride, none, 1 mM; sodium chloride, none, 100 mM; D2O, none, 10%; sodium azide, none, 0.05%; sodium phosphate, none, 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

AZARA, W Boucher - processing

ANALYSIS, W. Vranken, W. Boucher, T. Stevens, R. Fogh, A. Pajon, M. Llinas, E. Ulrich, J. Markley, J. Ionides, E. Laue - chemical shift assignment, data analysis, peak picking

CNS, A Brunger, P Adams, M Clore, P Gros, M Nilges and R Read - refinement, structure solution

TALOS, G Cornilescu, F Delaglio and A Bax - torsion angle prediction

ARIA, J Linge, S O'Donoghue and M Nilges - refinement, structure solution

Tensor2, P. Dosset, J-C. Hus, M. Blackledge, D. Marion - Model-free analysis

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 800 MHz