BMRB Entry 15707

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PDB ID:
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
MolProbity Validation Chart

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Title:
NMR solution structure of the split PH domain from Phospholipase C gamma 2
Deposition date:
2008-04-02
Original release date:
2008-09-16
Authors:
Harris, Richard; Bunney, Tom; Katan, Matilda; Driscoll, Paul
Citation:

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).
PubMed: 18728011

Assembly members:

Assembly members:
split_PH_domain_from_Phospholipase_C_gamma_2, polymer, 124 residues, 14229.8 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: pTriEx4

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts124
1H chemical shifts828

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1split PH domain from Phospholipase C gamma 21

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   GLYGLYGLYSERGLYGLYSERLYSLYSASP
2   GLUHISLYSGLNGLNGLYGLULEUTYRMET
3   TRPASPSERILEASPGLNLYSTRPTHRARG
4   HISTYRCYSALAILEALAASPALALYSLEU
5   SERPHESERASPASPILEGLUGLNTHRMET
6   GLUGLUASPASNPROLEUGLYSERLEUCYS
7   ARGGLYILELEUASPLEUASNTHRTYRASN
8   VALVALLYSALAPROGLNGLYLYSASNGLN
9   LYSSERPHEVALPHEILELEUGLUPROLYS
10   GLNGLNGLYASPPROPROVALGLUPHEALA
11   THRASPARGVALGLUGLULEUPHEGLUTRP
12   PHEGLNSERILEARGGLUILETHRTRPLYS
13   ILEASPTHRLYS

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:

NameSampleSample stateSample conditions
3D_15N-edited_NOESYsample_1isotropicsample_conditions_1
3D_13C-edited_NOESYsample_2isotropicsample_conditions_1
3D_13C-edited_aromatic_NOESYsample_2isotropicsample_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

Related Database Links:

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