BMRB Entry 15707

Name: NMR solution structure of the split PH domain from Phospholipase C gamma 2
Published: 2008-09-16

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PDB ID: 2k2j
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/BMR15707
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of the split PH domain from Phospholipase C gamma 2 PubMed: 18728011

Deposition date: 2008-04-02 Original release date: 2008-09-16

Authors: Harris, Richard; Bunney, Tom; Katan, Matilda; Driscoll, Paul

Citation: Walliser, C.; Retlich, M.; Harris, R.; Everett, K.; Josephs, M.; Vatter, P.; Esposito, D.; Driscoll, P.; Katan, M.; Gierschik, P.; Bunney, T.. "rac regulates its effector phospholipase Cgamma2 through interaction with a split pleckstrin homology domain" J. Biol. Chem. 283, 30351-30362 (2008).

Assembly members:
split_PH_domain_from_Phospholipase_C_gamma_2, polymer, 124 residues, 14229.8 Da.

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
split_PH_domain_from_Phospholipase_C_gamma_2: GGGSGGSKKDEHKQQGELYM WDSIDQKWTRHYCAIADAKL SFSDDIEQTMEEDNPLGSLC RGILDLNTYNVVKAPQGKNQ KSFVFILEPKQQGDPPVEFA TDRVEELFEWFQSIREITWK IDTK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	522
15N chemical shifts	124
1H chemical shifts	828

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	split PH domain from Phospholipase C gamma 2	1

Entities:

Entity 1, split PH domain from Phospholipase C gamma 2 124 residues - 14229.8 Da.

GGGSGGS is part of the tag residues and has not been assigned. Residues K8-E52 are equivalent to 471-515 and residues D53-K124 are equivalent to 842-913 in the phospholipase C gamma 2 sequence.

1

GLY

SER

GLY

SER

LYS

ASP

2

GLU

HIS

LYS

GLN

GLY

GLU

LEU

TYR

MET

3

TRP

ASP

SER

ILE

ASP

GLN

LYS

TRP

THR

ARG

4

HIS

TYR

CYS

ALA

ILE

ALA

ASP

ALA

LYS

LEU

5

SER

PHE

SER

ASP

ILE

GLU

GLN

THR

MET

6

GLU

ASP

ASN

PRO

LEU

GLY

SER

LEU

CYS

7

ARG

GLY

ILE

LEU

ASP

LEU

ASN

THR

TYR

ASN

8

VAL

LYS

ALA

PRO

GLN

GLY

LYS

ASN

GLN

9

LYS

SER

PHE

VAL

PHE

ILE

LEU

GLU

PRO

LYS

10

GLN

GLY

ASP

PRO

VAL

GLU

PHE

ALA

11

THR

ASP

ARG

VAL

GLU

LEU

PHE

GLU

TRP

12

PHE

GLN

SER

ILE

ARG

GLU

ILE

THR

TRP

LYS

13

ILE

ASP

THR

LYS

Samples:

sample_1: split PH domain from Phospholipase C gamma 2, [U-15N], 0.8-1.0 mM; Na phosphate buffer 25 mM; NaCl 150 mM; EDTA 1 mM; DTT 5 mM

sample_2: split PH domain from Phospholipase C gamma 2, [U-13C; U-15N], 0.8-1.0 mM; Na phosphate buffer 25 mM; NaCl 150 mM; EDTA 1 mM; DTT 5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-edited_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-edited_NOESY	sample_2	isotropic	sample_conditions_1
3D_13C-edited_aromatic_NOESY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

Varian Inova 600 MHz
Varian UnityPlus 500 MHz
Bruker Avance 700 MHz
Varian Inova 800 MHz

Biological Magnetic Resonance Data Bank