BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5310

Title: Backbone and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain complexed with a PDGFR-derived phosphopeptide   PubMed: 8181064

Deposition date: 2002-03-04 Original release date: 2008-07-17

Authors: Forman-Kay, Julie

Citation: Pascal, Steve; Singer, Alex; Gish, Gerry; Yamazaki, Toshio; Shoelson, Steven; Pawson, Tony; Kay, Lewis; Forman-Kay, Julie. "Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide "  Cell 77, 461-472 (1994).

Assembly members:
PLCC SH2, polymer, 105 residues, Formula weight is not available
PDGFR-derived phosphopeptide, residues 1018 to 1029, polymer, 12 residues, 261.168 Da.
PTR, non-polymer, 261.168 Da.

Natural source:   Common Name: Cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

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

Entity Sequences (FASTA):
PLCC SH2: GSPGIHESKEWYHASLTRAQ AEHMLMRVPRDGAFLVRKRN EPNSYAISFRAEGKIKHCRV QQEGQTVMLGNSEFDSLVDL ISYYEKHPLYRKMKLRYPIN EENSS
PDGFR-derived phosphopeptide, residues 1018 to 1029: DNDXIIPLPDPK

Data sets:
Data typeCount
1H chemical shifts781
13C chemical shifts460
15N chemical shifts133

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

SWISS-PROT Q62077 P08487 P19174 P10686
REF XP_514650.2 XP_001500255.1 XP_001087295.1 NP_002651.2 XP_542998.2
PRF 1404383A
GenBank EDL96615.1 ABK42331.1 EDL96614.1 EAW75989.1 EAW75993.1
EMBL CAM23068.1 CAM28260.1 CAA68406.1 CAM23067.1 CAA18537.1
DBJ BAE06110.1 BAG10236.1 BAE21990.1
PDB 2PLE 2PLD 2FCI
BMRB 5318

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts