BMRB Entry 15914

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for Binder of Arl2 (BART)
Published: 2008-11-19

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15914

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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:

Backbone 1H, 13C and 15N Chemical Shift Assignments for Binder of Arl2 (BART)

Deposition date:

2008-08-08

Original release date:

2008-11-19

Authors:

Bailey, Laura; Campbell, Louise; Evetts, Katrina; Littlefield, Keily; Rajendra, Eeson; Nietlispach, Daniel; Owen, Darerca; Mott, Helen

Citation:

Citation: Bailey, Laura; Campbell, Louise; Evetts, Katrina; Littlefield, Keily; Rajendra, Eeson; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "The structure of binder of Arl2 (BART) reveals a novel G protein binding domain: Implications for function." J. Biol. Chem. 284, 992-999 (2009).
PubMed: 18981177

Assembly members:

Assembly members:
Binder of Arl2, polymer, 137 residues, 16024.985 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: pET 16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Binder of Arl2: HMDALEGESFALSFSSASDA EFDAVVGYLEDIIMDDEFQL LQRNFMDKYYLEFEDTEENK LIYTPIFNEYISLVEKYIEE QLLQRIPEFNMAAFTTTLQH HKDEVAGDIFDMLLTFTDFL AFKEMFLDYRAEKEGRG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	576
15N chemical shifts	133
1H chemical shifts	906

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Binder of Arl2	1

Entities:

Entity 1, Binder of Arl2 137 residues - 16024.985 Da.

1

HIS

MET

ASP

ALA

LEU

GLU

GLY

GLU

SER

PHE

2

ALA

LEU

SER

PHE

SER

ALA

SER

ASP

ALA

3

GLU

PHE

ASP

ALA

VAL

GLY

TYR

LEU

GLU

4

ASP

ILE

MET

ASP

GLU

PHE

GLN

LEU

5

LEU

GLN

ARG

ASN

PHE

MET

ASP

LYS

TYR

6

LEU

GLU

PHE

GLU

ASP

THR

GLU

ASN

LYS

7

LEU

ILE

TYR

THR

PRO

ILE

PHE

ASN

GLU

TYR

8

ILE

SER

LEU

VAL

GLU

LYS

TYR

ILE

GLU

9

GLN

LEU

GLN

ARG

ILE

PRO

GLU

PHE

ASN

10

MET

ALA

PHE

THR

LEU

GLN

HIS

11

HIS

LYS

ASP

GLU

VAL

ALA

GLY

ASP

ILE

PHE

12

ASP

MET

LEU

THR

PHE

THR

ASP

PHE

LEU

13

ALA

PHE

LYS

GLU

MET

PHE

LEU

ASP

TYR

ARG

14

ALA

GLU

LYS

GLU

GLY

ARG

GLY

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
3D HNCO	sample_2	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
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1

PDB	2K9A 3DOE 3DOF
DBJ	BAE00391 BAG52057 BAG60900 BAK62297
EMBL	CAH91552
GB	AAD20633 AAH03087 AIC50989 EAW82913 EAW82914
REF	NP_001125911 NP_001233387 NP_001253957 NP_001271553 NP_036238
SP	Q4R930 Q5R9K8 Q9Y2Y0
AlphaFold	Q4R930 Q5R9K8 Q9Y2Y0

BMRB Entry 15914

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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