BMRB Entry 10319

Name: Solution structure of the PH domain of KIAA0640 protein from human
Published: 2010-03-11

Click here to enlarge.

PDB ID: 2dn6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10319
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the PH domain of KIAA0640 protein from human

Deposition date:

2009-03-11

Original release date:

2010-03-11

Authors:

Li, H.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of KIAA0640 protein from human" .

Assembly members:

Assembly members:
PH domain, polymer, 115 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: P050919-04

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGVLKQGYMMKKGHR RKNWTERWFVLKPNIISYYV SEDLKDKKGDILLDENCCVE SLPDKDGKKCLFLVKCFDKT FEISASDKKKKQEWIQAIHS TIHLLKLGSSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	508
15N chemical shifts	109
1H chemical shifts	797

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PH domain	1

Entities:

Entity 1, PH domain 115 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

VAL

LEU

LYS

2

GLN

GLY

TYR

MET

LYS

GLY

HIS

ARG

3

ARG

LYS

ASN

TRP

THR

GLU

ARG

TRP

PHE

VAL

4

LEU

LYS

PRO

ASN

ILE

SER

TYR

VAL

5

SER

GLU

ASP

LEU

LYS

ASP

LYS

GLY

ASP

6

ILE

LEU

ASP

GLU

ASN

CYS

VAL

GLU

7

SER

LEU

PRO

ASP

LYS

ASP

GLY

LYS

CYS

8

LEU

PHE

LEU

VAL

LYS

CYS

PHE

ASP

LYS

THR

9

PHE

GLU

ILE

SER

ALA

SER

ASP

LYS

10

LYS

GLN

GLU

TRP

ILE

GLN

ALA

ILE

HIS

SER

11

THR

ILE

HIS

LEU

LYS

LEU

GLY

SER

12

GLY

PRO

SER

GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.17 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 900 MHz

PDB	2DN6
DBJ	BAA31615 BAG09789 BAG53381 BAG65007
GB	AAF24486 AAF61403 AAH00616 AIC50910 EAW68582
REF	NP_001165885 NP_001284643 NP_055870 XP_002755082 XP_002822083
SP	Q9UH65
AlphaFold	Q9UH65