BMRB Entry 10313

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PDB ID: 2da0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10313
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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:

Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human

Deposition date:

2009-03-11

Original release date:

2010-03-11

Authors:

Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.; RIKEN, Structural

Citation:

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human" .

Assembly members:

Assembly members:
PH domain, polymer, 114 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: Cell-free synthesis Vector: P050801-06

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGYGSEKKGYLLKKS DGIRKVWQRRKCSVKNGILT ISHATSNRQPAKLNLLTCQV KPNAEDKKSFDLISHNRTYH FQAEDEQDYVAWISVLTNSK EEALTMAFSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	477
15N chemical shifts	111
1H chemical shifts	749

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PH domain	1

Entities:

Entity 1, PH domain 114 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

TYR

GLY

SER

2

GLU

LYS

GLY

TYR

LEU

LYS

SER

3

ASP

GLY

ILE

ARG

LYS

VAL

TRP

GLN

ARG

4

LYS

CYS

SER

VAL

LYS

ASN

GLY

ILE

LEU

THR

5

ILE

SER

HIS

ALA

THR

SER

ASN

ARG

GLN

PRO

6

ALA

LYS

LEU

ASN

LEU

THR

CYS

GLN

VAL

7

LYS

PRO

ASN

ALA

GLU

ASP

LYS

SER

PHE

8

ASP

LEU

ILE

SER

HIS

ASN

ARG

THR

TYR

HIS

9

PHE

GLN

ALA

GLU

ASP

GLU

GLN

ASP

TYR

VAL

10

ALA

TRP

ILE

SER

VAL

LEU

THR

ASN

SER

LYS

11

GLU

ALA

LEU

THR

MET

ALA

PHE

SER

GLY

12

PRO

SER

GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.18 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.932, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz