BMRB Entry 16681

Name: Solution NMR Structure of the SH3 Domain from the p85beta subunit of Phosphatidylinositol 3-kinase from H.sapiens. Northeast Structural Genomics Consortium Target HR5531E.
Published: 2010-02-22

Click here to enlarge.

PDB ID: 2kt1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16681
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 NMR Structure of the SH3 Domain from the p85beta subunit of Phosphatidylinositol 3-kinase from H.sapiens. Northeast Structural Genomics Consortium Target HR5531E.

Deposition date:

2010-01-15

Original release date:

2010-02-22

Authors:

Aramini, James; Ma, Li-Chung; Schauder, Curtis; Everett, John; Montelione, Gaetano

Citation:

Citation: Aramini, James; Ma, Li-Chung; Schauder, Curtis; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the SH3 Domain from the p85beta subunit of Phosphatidylinositol 3-kinase from H.sapiens. Northeast Structural Genomics Consortium Target HR5531E." To be published ., .-..

Assembly members:

Assembly members:
HR5531E, polymer, 88 residues, 9130.386 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: HR5531E-1-80-21.1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR5531E: MAGPEGFQYRALYPFRRERP EDLELLPGDVLVVSRAALQA LGVAEGGERCPQSVGWMPGL NERTRQRGDFPGTYVEFLGP LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	350
15N chemical shifts	73
1H chemical shifts	543

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR5531E	1

Entities:

Entity 1, HR5531E 88 residues - 9130.386 Da.

Contains additional C-terminal LEHHHHHH affinity tag

1

MET

ALA

GLY

PRO

GLU

GLY

PHE

GLN

TYR

ARG

2

ALA

LEU

TYR

PRO

PHE

ARG

GLU

ARG

PRO

3

GLU

ASP

LEU

GLU

LEU

PRO

GLY

ASP

VAL

4

LEU

VAL

SER

ARG

ALA

LEU

GLN

ALA

5

LEU

GLY

VAL

ALA

GLU

GLY

GLU

ARG

CYS

6

PRO

GLN

SER

VAL

GLY

TRP

MET

PRO

GLY

LEU

7

ASN

GLU

ARG

THR

ARG

GLN

ARG

GLY

ASP

PHE

8

PRO

GLY

THR

TYR

VAL

GLU

PHE

LEU

GLY

PRO

9

LEU

GLU

HIS

Samples:

sample_1: HR5531E, [U-100% 13C; U-100% 15N], 0.62 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 50 uM; DTT 10 mM; H2O 95%; D2O 5%

sample_2: HR5531E, [U-5% 13C; U-100% 15N], 0.50 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 50 uM; DTT 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
1D 1H-15N T1 and T2	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC high res. (L/V methyl stereoassignment)	sample_2	isotropic	sample_conditions_1
2D 1H-15N hetNOE	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.112, Goddard - data analysis, peak picking

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

PSVS v1.4, Bhattacharya and Montelione - structure quality analysis

TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints

PDBStat v5.1, Tejero and Montelione - PDB coordinate analysis

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	2KT1 3O5Z
DBJ	BAG11075
EMBL	CAA56868
GB	AAA79510 AAD22671 AAH32647 AAH70082 AAH90249
REF	NP_001244981 NP_005018 NP_777001 XP_002761945 XP_003275871
SP	O00459 P23726
TPG	DAA28159
AlphaFold	O00459 P23726