BMRB Entry 11087

Name: Solution structure of the PH domain of Kindlin-3 from human
Published: 2011-01-14

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PDB ID: 2ys3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11087
MolProbity Validation Chart

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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 Kindlin-3 from human

Deposition date:

2010-01-15

Original release date:

2011-01-14

Authors:

Li, H.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of Kindlin-3 from human" .

Assembly members:

Assembly members:
PH domain, UNP residues 349-478, polymer, 137 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 Host organism: E. coli - cell free Vector: P060904-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain, UNP residues 349-478: GSSGSSGIPELKDHLRIFRP RKLTLKGYRQHWVVFKETTL SYYKSQDEAPGDPIQQLNLK GCEVVPDVNVSGQKFCIKLL VPSPEGMSEIYLRCQDEQQY ARWMAGCRLASKGRTMADSS YTSEVQAILAFLSLQRT

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	608
15N chemical shifts	134
1H chemical shifts	956

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PH domain, UNP residues 349-478	1

Entities:

Entity 1, PH domain, UNP residues 349-478 137 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ILE

PRO

GLU

2

LEU

LYS

ASP

HIS

LEU

ARG

ILE

PHE

ARG

PRO

3

ARG

LYS

LEU

THR

LEU

LYS

GLY

TYR

ARG

GLN

4

HIS

TRP

VAL

PHE

LYS

GLU

THR

LEU

5

SER

TYR

LYS

SER

GLN

ASP

GLU

ALA

PRO

6

GLY

ASP

PRO

ILE

GLN

LEU

ASN

LEU

LYS

7

GLY

CYS

GLU

VAL

PRO

ASP

VAL

ASN

VAL

8

SER

GLY

GLN

LYS

PHE

CYS

ILE

LYS

LEU

9

VAL

PRO

SER

PRO

GLU

GLY

MET

SER

GLU

ILE

10

TYR

LEU

ARG

CYS

GLN

ASP

GLU

GLN

TYR

11

ALA

ARG

TRP

MET

ALA

GLY

CYS

ARG

LEU

ALA

12

SER

LYS

GLY

ARG

THR

MET

ALA

ASP

SER

13

TYR

THR

SER

GLU

VAL

GLN

ALA

ILE

LEU

ALA

14

PHE

LEU

SER

LEU

GLN

ARG

THR

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.18 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 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 v20031121, Delaglio, F. - processing

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

Kujira v0.9820, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2YS3
DBJ	BAC04220
GB	AAH04347 AAH13366 AAH15584 AAI09489 AAM19736
REF	NP_001032695 NP_113659 XP_001118313 XP_002821634 XP_003639703
SP	Q32LP0
TPG	DAA13656
AlphaFold	Q32LP0