BMRB Entry 26625

Name: PH domain of the Arf GAP ASAP1
Published: 2015-09-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26625

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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: PH domain of the Arf GAP ASAP1 PubMed: 26365802

Deposition date: 2015-08-06 Original release date: 2015-09-29

Authors: Li, Yifei; Byrd, Andrew

Citation: Jian, Xiaoying; Tang, Wai-Kwan; Zhai, Peng; Roy, Neeladri; Luo, Ruibai; Gruschus, James; Yohe, Marielle; Chen, Pei-Wen; Li, Yifei; Byrd, Andrew; Xia, Di; Randazzo, Paul. "Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1" Structure 23, 1977-1988 (2015).

Assembly members:
ASAP1_PH_domain, polymer, 111 residues, Formula weight is not available

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
ASAP1_PH_domain: EKKGFLLKKSDGIRKVWQRR KCAVKNGILTISHATSNRQP AKLNLLTCQVKPNAEDKKSF DLISHNRTYHFQAEDEQDYI AWISVLTNSKEEALTMAFRG EQSTGENSLED

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	1
15N chemical shifts	97
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ASAP1 PH domain	1

Entities:

Entity 1, ASAP1 PH domain 111 residues - Formula weight is not available

residue numbering begins at 341

1

GLU

LYS

GLY

PHE

LEU

LYS

SER

2

ASP

GLY

ILE

ARG

LYS

VAL

TRP

GLN

ARG

3

LYS

CYS

ALA

VAL

LYS

ASN

GLY

ILE

LEU

THR

4

ILE

SER

HIS

ALA

THR

SER

ASN

ARG

GLN

PRO

5

ALA

LYS

LEU

ASN

LEU

THR

CYS

GLN

VAL

6

LYS

PRO

ASN

ALA

GLU

ASP

LYS

SER

PHE

7

ASP

LEU

ILE

SER

HIS

ASN

ARG

THR

TYR

HIS

8

PHE

GLN

ALA

GLU

ASP

GLU

GLN

ASP

TYR

ILE

9

ALA

TRP

ILE

SER

VAL

LEU

THR

ASN

SER

LYS

10

GLU

ALA

LEU

THR

MET

ALA

PHE

ARG

GLY

11

GLU

GLN

SER

THR

GLY

GLU

ASN

SER

LEU

GLU

12

ASP

Samples:

sample_1: ASAP1 PH domain, [U-99% 13C; U-99% 15N], 250 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts