BMRB Entry 10278

Click here to enlarge.

PDB ID: 2d9v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10278
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 Pleckstrin homology domain-containing protein family B member 1 from mouse

Deposition date:

2008-12-15

Original release date:

2009-12-14

Authors:

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

Citation:

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of Pleckstrin homology domain-containing protein family B member 1 from mouse" .

Assembly members:

Assembly members:
PH domain, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P050302-02

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGLVRGGWLWRQSSI LRRWKRNWFALWLDGTLGYY HDETAQDEEDRVVIHFNVRD IKVGQECQDVQPPEGRSRDG LLTVNLREGSRLHLCAETRD DAIAWKTALMEANSTPAPAG ATVPSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	518
15N chemical shifts	129
1H chemical shifts	815

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 130 residues - Formula weight is not available

1	GLY	SER	SER	GLY	SER	SER	GLY	LEU	VAL	ARG
2	GLY	GLY	TRP	LEU	TRP	ARG	GLN	SER	SER	ILE
3	LEU	ARG	ARG	TRP	LYS	ARG	ASN	TRP	PHE	ALA
4	LEU	TRP	LEU	ASP	GLY	THR	LEU	GLY	TYR	TYR
5	HIS	ASP	GLU	THR	ALA	GLN	ASP	GLU	GLU	ASP
6	ARG	VAL	VAL	ILE	HIS	PHE	ASN	VAL	ARG	ASP
7	ILE	LYS	VAL	GLY	GLN	GLU	CYS	GLN	ASP	VAL
8	GLN	PRO	PRO	GLU	GLY	ARG	SER	ARG	ASP	GLY
9	LEU	LEU	THR	VAL	ASN	LEU	ARG	GLU	GLY	SER
10	ARG	LEU	HIS	LEU	CYS	ALA	GLU	THR	ARG	ASP
11	ASP	ALA	ILE	ALA	TRP	LYS	THR	ALA	LEU	MET
12	GLU	ALA	ASN	SER	THR	PRO	ALA	PRO	ALA	GLY
13	ALA	THR	VAL	PRO	SER	GLY	PRO	SER	SER	GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.12 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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

1	GLY	SER	SER	GLY	SER	SER	GLY	LEU	VAL	ARG
2	GLY	GLY	TRP	LEU	TRP	ARG	GLN	SER	SER	ILE
3	LEU	ARG	ARG	TRP	LYS	ARG	ASN	TRP	PHE	ALA
4	LEU	TRP	LEU	ASP	GLY	THR	LEU	GLY	TYR	TYR
5	HIS	ASP	GLU	THR	ALA	GLN	ASP	GLU	GLU	ASP
6	ARG	VAL	VAL	ILE	HIS	PHE	ASN	VAL	ARG	ASP
7	ILE	LYS	VAL	GLY	GLN	GLU	CYS	GLN	ASP	VAL
8	GLN	PRO	PRO	GLU	GLY	ARG	SER	ARG	ASP	GLY
9	LEU	LEU	THR	VAL	ASN	LEU	ARG	GLU	GLY	SER
10	ARG	LEU	HIS	LEU	CYS	ALA	GLU	THR	ARG	ASP
11	ASP	ALA	ILE	ALA	TRP	LYS	THR	ALA	LEU	MET
12	GLU	ALA	ASN	SER	THR	PRO	ALA	PRO	ALA	GLY
13	ALA	THR	VAL	PRO	SER	GLY	PRO	SER	SER	GLY

1	GLY	SER	SER	GLY	SER	SER	GLY	LEU	VAL	ARG
2	GLY	GLY	TRP	LEU	TRP	ARG	GLN	SER	SER	ILE
3	LEU	ARG	ARG	TRP	LYS	ARG	ASN	TRP	PHE	ALA
4	LEU	TRP	LEU	ASP	GLY	THR	LEU	GLY	TYR	TYR
5	HIS	ASP	GLU	THR	ALA	GLN	ASP	GLU	GLU	ASP
6	ARG	VAL	VAL	ILE	HIS	PHE	ASN	VAL	ARG	ASP
7	ILE	LYS	VAL	GLY	GLN	GLU	CYS	GLN	ASP	VAL
8	GLN	PRO	PRO	GLU	GLY	ARG	SER	ARG	ASP	GLY
9	LEU	LEU	THR	VAL	ASN	LEU	ARG	GLU	GLY	SER
10	ARG	LEU	HIS	LEU	CYS	ALA	GLU	THR	ARG	ASP
11	ASP	ALA	ILE	ALA	TRP	LYS	THR	ALA	LEU	MET
12	GLU	ALA	ASN	SER	THR	PRO	ALA	PRO	ALA	GLY
13	ALA	THR	VAL	PRO	SER	GLY	PRO	SER	SER	GLY

1	GLY	SER	SER	GLY	SER	SER	GLY	LEU	VAL	ARG
2	GLY	GLY	TRP	LEU	TRP	ARG	GLN	SER	SER	ILE
3	LEU	ARG	ARG	TRP	LYS	ARG	ASN	TRP	PHE	ALA
4	LEU	TRP	LEU	ASP	GLY	THR	LEU	GLY	TYR	TYR
5	HIS	ASP	GLU	THR	ALA	GLN	ASP	GLU	GLU	ASP
6	ARG	VAL	VAL	ILE	HIS	PHE	ASN	VAL	ARG	ASP
7	ILE	LYS	VAL	GLY	GLN	GLU	CYS	GLN	ASP	VAL
8	GLN	PRO	PRO	GLU	GLY	ARG	SER	ARG	ASP	GLY
9	LEU	LEU	THR	VAL	ASN	LEU	ARG	GLU	GLY	SER
10	ARG	LEU	HIS	LEU	CYS	ALA	GLU	THR	ARG	ASP
11	ASP	ALA	ILE	ALA	TRP	LYS	THR	ALA	LEU	MET
12	GLU	ALA	ASN	SER	THR	PRO	ALA	PRO	ALA	GLY
13	ALA	THR	VAL	PRO	SER	GLY	PRO	SER	SER	GLY